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Last modified: 19 April 1999

Bibliography on structural studies of cytochrome c oxidase
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  1. Aasa, R., Albracht, P.J., Falk, K.­E., Lanne, B. and Vänngård, T. (1976) EPR signals from cytochrome c oxidase. Biochim. Biophys. Acta 422, 260-272.
  2. Adar, F. and Erecinska, M. (1978) Resonance Raman spectra of whole mitochondria. Biochemistry 17, 5484-5488.
  3. Adar, F. and Erecinska, M. (1979) Photoreductive titration of the resonance Raman spectra of cytochrome oxidase in whole mitochondria. Biochemistry 18, 1825-1829.
  4. Adar, F. and Yonetani, T. (1978) Resonance Raman spectra of cytochrome oxidase. Evidence for photoreduction by laser photons in resonance with the Soret band. Biochim. Biophys. Acta 502, 80-86.
  5. Ädelroth, P., Mitchell, D.M., Gennis, R.B. and Brzezinski, P. (1997) Factors determining electron­transfer rates in cytochrome c oxidase: Studies of the FQ(I­391) mutant of the Rhodobacter sphaeroides enzyme. Biochemistry 36, 11787-11796.
  6. Akey, C.W., Moffat, K., Wharton, D.C. and Edelstein, S.J. (1980) Characterization of crystals of a cytochrome oxidase (nitrite reductase) from Pseudomonas aeruginosa by x­ray diffraction and electron microscopy. J. Mol. Biol. 136, 19-43.
  7. Alben, J.O., Moh, P.P., Fiamingo, F.G. and Altschuld, R.A.(1981) Cytochrome oxidase a3 heme and copper observed by low­temperature Fourier transform infrared spectroscopy of the CO complex. Proc. Natl. Acad. Sci. USA 78, 234-237.
  8. Allen, L.A., Zhao, X.­J., Caughey, W.S. and Poyton, R.O. (1995) Isoforms of yeast cytochrome c oxidase subunit V affect the binuclear reaction center and alter the kinetics of interaction with the isoforms of yeast cytochrome c. J. Biol. Chem. 270, 110-118.
  9. Andrew, C.R., Fraczkiewicz, R., Czernuszewicz, R.S., Lappalainen, P., Saraste, M. and Sanders­Loehr, J. (1996) Identification and description of copper-thiolate vibrations in the dinuclear CuA site of cytochrome c oxidase. J. Am. Chem. Soc. 118, 10436-10445.
  10. Anemuller, S., Bill, E., Schafer, G., Trautwein, A.X. and Teixeira, M. (1992) EPR studies of cytochrome aa3 from Sulfolobus acidocaldarius. Evidence for a binuclear center in archaebacterial terminal oxidase. Eur. J. Biochem. 210, 133-138.
  11. Argade, P.V., Ching, Y.­C., Sassaroli, M. and Rousseau, D.L. (1986) Accessibility of the cytochrome a heme in cytochrome c oxidase to exchangeable protons. J. Biol. Chem. 261, 5969-5973.
  12. Arrondo, J.L., Castresana, J., Valpuesta, J.M. and Goni, F.M. (1994) Structure and thermal denaturation of crystalline and noncrystalline cytochrome oxidase as studied by infrared spectroscopy. Biochemistry 33, 11650-11655.
  13. Babcock, G.T. and Callahan, P.M. (1983) Redox­linked hydrogen bond strength changes in cytochrome a: Implications for a cytochrome oxidase proton pump. Biochemistry 22, 2314-2319.
  14. Babcock, G.T. and Salmeen, I. (1979) Resonance Raman spectra and optical properties of oxidized cytochrome oxidase. Biochemistry 18, 2493-2498.
  15. Babcock, G.T., Vickery, L.E. and Palmer, G. (1976) Electronic state of heme in cytochrome oxidase. I. Magnetic circular dichroism of the isolated enzyme and its derivatives. J. Biol. Chem. 251, 7907-7919.
  16. Babcock, G.T., Vickery, L.E. and Palmer, G. (1978) The electronic state of heme in cytochrome oxidase. II. Oxidation­reduction potential interactions and heme iron spin state behavior observed in reductive titrations. J. Biol. Chem. 253, 2400-2411.
  17. Babcock, G.T., Callahan, P.M., Ondrias, M.R. and Salmeen, I. (1981) Coordination geometries and vibrational properties of cytochromes alpha and alpha3 in cytochrome oxidase from Soret excitation Raman spectroscopy. Biochemistry 20, 959-966.
  18. Baker, G.M. and Palmer, G. (1987) Effect of high pH on the spectral and catalytic properties of beef heart cytochrome oxidase. Biochemistry 26, 3038-3044.
  19. Behr, J., Hellwig, P., Mäntele, W. and Michel, H. (1998) Redox dependent changes at the heme propionates in cytochrome c oxidase from Paracoccus denitrificans: Direct evidence from FTIR difference spectroscopy in combination with heme propionate 13C labeling. Biochemistry 37, 7400-7406.
  20. Beinert, H., Hartzell, C.R., van Gelder, B.F., Ganapathy, K., Mason, H.S. and Wharton, D.C. (1970) A reappraisal of copper depletion from cytochrome c oxidase. J. Biol. Chem. 245, 225-229.
  21. Beinert, H., Hansen, R.E. and Hartzell, C.R. (1976) Kinetic studies on cytochrome c oxidase by combined EPR and reflectance spectroscopy after rapid freezing. Biochim. Biophys. Acta 423, 339-355.
  22. Beinert, H., Shaw, R.H., Hansen, R.E. and Hartzell, C.R. (1980) Studies on the origin of the near­infrared (800-900 nm) absorption of cytochrome c oxidase. Biochim. Biophys. Acta 591, 458-470.
  23. Bertini, I., Bren, K.L., Clemente, A., Fee, J.A., Gray, H.B., Luchinat, C., Malmström, B.G., Richards, J.H., Sanders, D. and Slutter, C.E. (1996) The CuA center of a soluble domain from Thermus cytochrome ba3. An NMR investigation of the paramagnetic protein. J. Am. Chem. Soc. 118, 11658-11659.
  24. Blackburn, N.J., Barr, M.E., Woodruff, W.H., van der Ooost, J. and de Vries, S. (1994) Metal-metal bonding in biology: EXAFS evidence for a 2.5 Å copper-copper bond in the CuA center of cytochrome oxidase. Biochemistry 33, 10401-10407.
  25. Blackburn, N.J., de Vries, S., Barr, M.E., Houser, R.P., Tolman, W.B., Sanders, D. and Fee, J.A. (1997) X­ray absorption studies on the mixed­valence and fully reduced forms of the soluble CuA domains of cytochrome c oxidase. J. Am. Chem. Soc. 119, 6135-6143.
  26. Blatt, Y., Benko, B., Pecht, I. and Vuk­Pavlovic, S. (1981) Proton magnetic resonance relaxation in Pseudomonas aeruginosa cytochrome oxidase solutions. J. Biol. Chem. 256, 2197-2301.
  27. Blum, H., Harmon, H.J., Leigh, J.S., Salerno, J.C. and Chance, B. (1978) The orientation of a heme of cytochrome c oxidase in submitochondrial particles. Biochim. Biophys. Acta 502, 1-10.
  28. Blum, H., Leigh, J.S. and Ohnishi, T. (1980) Effect of dysprosium on the spin­lattice relaxation time of cytochrome c and cytochrome a. Biochim. Biophys. Acta 626, 31-40.
  29. Bocian, D.F., Lemley, A.T., Petersen, N.O., Brudvig, G.W. and Chan, S.I. (1979) Resonance Raman spectra of cytochrome c oxidase. Excitation in the 600­nm region. Biochemistry 18, 4396-4402.
  30. Bose, S., Hendler, R.W., Shrager, R.I., Chan, S.I. and Smith, P.D. (1997) Multichannel analysis of single­turnover kinetics of cytochrome aa3 reduction of O2. Biochemistry 36, 2439-2449.
  31. Brittain, T., Springall, J., Greenwood, C. and Thomson, A.J. (1976) Low­temperature studies on mixed­valence cytochrome oxidase by using magnetic circular dichroism. Biochem. J. 159, 811-813.
  32. Brittain, T., Greenwood, C. and Johnson, A. (1977) Mixed­valence cytochrome oxidase-formate complex. A steady­state intermediate. Biochem. J. 167, 531-534.
  33. Brudvig, G.W., Bocian, D.F., Gamble, R.C. and Chan, S.I. (1980) Evidence for the absence of photoreduction of the metal centers of cytochrome c oxidase by X­irradiation. Biochim. Biophys. Acta 624, 78-89.
  34. Brudvig, G.W., Stevens, T.H., Morse, R.H. and Chan, S.I. (1981) Conformations of oxidized cytochrome c oxidase. Biochemistry 20, 3912-3921.
  35. Brudvig, G.W., Blair, D.F. and Chan, S.I. (1984) Electron spin relaxation of CuA and cytochrome a in cytochrome c oxidase. Comparison to heme, copper, and sulfur radical complexes. J. Biol. Chem. 259, 11001-11009.
  36. Brunori, M. and Gibson, Q.H. (1983) Oxygen activation by cytochrome oxidase: a new spectral intermediate observed by flow­flash. EMBO J. 2, 2025-2026.
  37. Burgess, J.D., Jones, V.W., Porter, M.D., Rhoten, M.C. and Hawkridge, F.M. (1998) Scanning force microscopy images of cytochrome c oxidase immobilized in an electrode­supported lipid bilayer membrane. Langmuir 14, 6628-6631.
  38. Calhoun, M.W., Thomas, J.W., Hill, J.J., Hosler, J.P., Shapleigh, J.P., Tecklenburg, M.M.J., Ferguson­Miller, S., Babcock, G.T., Alben, J.O. and Gennis, R.B. (1993) Identity of the axial ligand of the high­spin heme in cytochrome oxidase: spectroscopic characterization of mutants in the bo­type oxidase of Escherichia coli and the aa3­type oxidase of Rhodobacter sphaeroides. Biochemistry 32, 10905-10911.
  39. Capaldi, R.A. and Zhang, Y.Z. (1986) Structure of beef heart cytochrome­c oxidase obtained by combining studies of two­dimensional crystals with biochemical experiments. Methods Enzymol. 126, 22-31.
  40. Carithers, R.P. and Palmer, G. (1981) Characterization of the potentiometric behavior of soluble cytochrome oxidase by magnetic circular dichroism. Evidence in support of heme-heme interaction. J. Biol. Chem. 256, 7967-7976.
  41. Carter, K. and Palmer, G. (1982) Models of the two heme centers in cytochrome oxidase. The optical properties of cytochrome a and a3. J. Biol. Chem. 257, 13507-13514.
  42. Carter, K.R., Antalis, T.M., Palmer, G., Ferris, N.S. and Woodruff, W.H. (1981) Spectroscopic characterization of compound C and related derivatives of cytochrome oxidase. Proc. Natl. Acad. Sci. USA 78, 1652-1655.
  43. Centeno, J.A. (1992) Evidence of dithionite contribution to the low­frequency resonance Raman spectrum of reduced and mixed­valence cytochrome c oxidase. Arch. Biochem. Biophys. 292, 624-628.
  44. Chance, B. and Leigh, J.S. (1977) Oxygen intermediates and mixed valence states of cytochrome oxidase: infrared absorption difference spectra of compounds A, B, and C of cytochrome oxidase and oxygen. Proc. Natl. Acad. Sci. USA 74, 4777-4780.
  45. Chance, B., Saronio, S. and Leigh, J.S. (1979) Compound C2, a product of the reaction of oxygen and the mixed­valence state of cytochrome oxidase. Optical evidence for a type­I copper. Biochem. J. 177, 931-941.
  46. Cheesman, M.R., Zumft, W.G. and Thomson, A.J. (1998) The MCD and EPR of the heme centers of nitric oxide reductase from Pseudomonas stutzeri: Evidence that the enzyme is structurally related to the heme-copper oxidase. Biochemistry 37, 3994-4000.
  47. Ching, Y.­C., Argade, P.V. and Rousseau, D.L. (1985) Resonance Raman spectra of CN¯­bound cytochrome oxidase: spectral isolation of cytochromes a2+, a32+, and a32+CN¯. Biochemistry 24, 4938-4946.
  48. Chupin, V., Leenhouts, J.M., de Kroon, A.I. and de Kruijff, B. (1995) Cardiolipin modulates the secondary structure of the presequence peptide of cytochrome oxidase subunit IV: a 2D 1H­NMR study. FEBS Lett. 373, 239-244.
  49. Chupin, V., Leenhouts, J.M., de Kroon, A.I.P.M. and de Kruijff, B. (1996) Secondary structure and topology of a mitochondrial presequence peptide associated with negatively charged micelles. A 2D 1H­NMR study. Biochemistry 35, 3141-3146.
  50. Cline, J., Reinhammar, B., Jensen, P., Venters, R. and Hoffman, B.M. (1983) Coordination environment for the type 3 copper center of tree laccase and CuB of cytochrome c oxidase as determined by electron nuclear double resonance. J. Biol. Chem. 258, 5124-5128.
  51. Clore, G.M. and Chance, E.M. (1979) Low­temperature kinetics of the reactions of fully reduced membrane­bound cytochrome oxidase with oxygen in the Soret, alpha and near­infrared regions. Biochem. J. 177, 613-621.
  52. Clore, G.M., Andréasson, L.­E., Karlsson, B., Aasa, R. and Malmström, B.G. (1980a) Characterization of the low­temperature intermediates of the reaction of fully reduced soluble cytochrome oxidase with oxygen by electron­paramagnetic­resonance and optical spectroscopy. Biochem. J. 185, 139-154.
  53. Clore, G.M., Andréasson, L.­E., Karlsson, B., Aasa, R. and Malmström, B.G. (1980b) Characterization of the intermediates in the reaction of mixed­valence state soluble cytochrome oxidase with oxygen at low temperatures by optical and electron­paramagnetic­resonance spectroscopy. Biochem. J. 185, 155-167.
  54. Collman, J.P., Rapta, M., Bröring, M., Raptova, L., Schwenninger, R., Boitrel, B., Fu, L. and L'Her, M. (1999) Close structural analogues of the cytochrome c oxidase Fea3/CuB center show clean 4e¯ electroreduction of O2 to H2O at physiological pH. J. Am. Chem. Soc. 121, 1387-1388.
  55. Cooper, C.E., Pezeshk, A., Torres, J., Wilson, M. and Symons, M.R. (1996) A new EPR signal from cytochrome oxidase - Evidence for conformational flexibility at the CuB site? Biochem. Soc. Trans. 24, 465S.
  56. Copeland, R.A. and Spiro, T.G. (1986) Resonance Raman evidence for an exchangeable protein hydrogen associated with the heme a group of cytochrome oxidase. FEBS Lett. 197, 239-243.
  57. Copeland, R.A., Naqui, A., Chance, B. and Spiro, T.G. (1985) Resonance Raman spectroscopy and enhanced photoreducibility for the 420 nm pulsed form of cytochrome oxidase. FEBS Lett. 182, 375-379.
  58. Crum, J., Gruys, K.J. and Frey, T.G. (1994) Electron microscopy of cytochrome c oxidase crystals: labeling of subunit III with a monomaleimide undecagold cluster compound. Biochemistry 33, 13719-13726.
  59. Das, T.K. and Mazumdar, S. (1993) Time­resolved study of tryptophan fluorescence in vesicle reconstituted cytochrome oxidase. Effect of redox transition. FEBS Lett. 336, 211-214.
  60. Das, T.K. and Mazumdar, S. (1994) Conformational change due to reduction of cytochrome­c oxidase in lauryl maltoside: picosecond time­resolved tryptophan fluorescence studies on the native and heat modified enzyme. Biochim. Biophys. Acta 1209, 227-237 [published erratum Biochim. Biophys. Acta 1249, 205 (1995)].
  61. Das, T.K., Pecoraro, C., Tomson, F.L., Gennis, R.B. and Rousseau, D.L. (1998) The post­translational modification in cytochrome c oxidase is required to establish a functional environment of the catalytic site. Biochemistry 37, 14471-14476.
  62. Davydov, R.M. (1980) Absorption and magnetic circular dichroism spectra of heme proteins in nonequilibrium states. VI. Cytochrome c­oxidase. Mol. Biol. (Moscow) 14, 272-277.
  63. Deatherage, J.F., Henderson, R. and Capaldi, R.A. (1982) Three­dimensional structures of cytochrome c oxidase vesicle crystals in negative stain. J. Mol. Biol. 158, 487-499.
  64. de Paula, J.C., Peiffer, W.E., Ingle, R.T., Centeno, J.A., Ferguson­Miller, S. and Babcock, G.T. (1990) Hemes a and a3 environments of plant cytochrome c oxidase. Biochemistry 29, 8702-8706.
  65. Dispirito, A.A., Lipscomb, J.D. and Hooper, A.B. (1986) Cytochrome aa3 from Nitrosomonas europaea. J. Biol. Chem. 261, 17048-17056.
  66. Dodson, E.D., Zhao, X.­J., Caughey, W.S. and Elliott, C.M. (1996) Redox dependent interactions of the metal sites in carbon monoxide­bound cytochrome c oxidase monitored by infrared and UV/visible spectroelectrochemical methods. Biochemistry 35, 444-452.
  67. Dong, A., Huang, P., Zhao, X.­J., Sampath, V. and Caughey, W.S. (1994) Characterization of sites occupied by the anesthetic nitrous oxide within proteins by infrared spectroscopy. J. Biol. Chem. 269, 23911-23917.
  68. Dunham, W.R., Sands, R.H., Shaw, R.W. and Beinert, H. (1983) Multiple frequency EPR studies on three forms of oxidized cytochrome c oxidase. Biochim. Biophys. Acta 748, 73-85.
  69. Dyer, R.B., Peterson, K.A., Stoutland, P.O. and Woodruff, W.H. (1994) Picosecond infrared study of the photodynamics of carbonmonoxy­cytochrome c oxidase. Biochemistry 33, 500-507.
  70. Echabe, I., Haltia, T., Freire, E., Goni, F.M. and Arrondo, J.L. (1995) Subunit III of cytochrome c oxidase influences the conformation of subunits I and II: an infrared study. Biochemistry 34, 13565-13569.
  71. Edwards, A.M., Chupa, J.A., Strongin, R.M., Smith, A.B., III, Blasie, J.K. and Bean, J.C. (1997) Vectorially­oriented monolayers of cytochrome oxidase: Fabrication and profile structures. Langmuir 13, 1634-1643.
  72. Eglinton, D.G., Johnson, M.K., Thomson, A.J., Gooding, P.E. and Greenwood, C. (1980) Near­infrared magnetic and natural circular dichroism of cytochrome c oxidase. Biochem. J. 191, 319-331.
  73. Einarsdóttir, Ó. and Caughey, W.S. (1988) Interactions of the anesthetic nitrous oxide with bovine heart cytochrome c oxidase. Effects on protein structure, oxidase activity, and other properties. J. Biol. Chem. 263, 9199-9205.
  74. Einarsdóttir, Ó., Choc, M.G., Weldon, S. and Caughey, W.S. (1988) The site and mechanism of dioxygen reduction in bovine heart cytochrome c oxidase. J. Biol. Chem. 263, 13641-13654.
  75. Einarsdóttir, Ó., Killough, P.M., Fee, J.A. and Woodruff, W.H. (1989) An infrared study of the binding and photodissociation of carbon monoxide in cytochrome ba3 from Thermus thermophilus. J. Biol. Chem. 264, 2405-2408.
  76. Einarsdóttir, Ó., Georgiadis, K.E. and Dawes, T.D. (1992a) Evidence for a band III analogue in the near­infrared absorption spectra of cytochrome c oxidase. Biochem. Biophys. Res. Commun. 184, 1035-1041.
  77. Einarsdóttir, Ó., Dawes, T.D. and Georgiadis, K.E. (1992b) New transients in the electron­transfer dynamics of photolyzed mixed­valence CO-cytochrome c oxidase. Proc. Natl. Acad. Sci. USA 89, 6934-6937.
  78. Einarsdóttir, Ó., Dyer, R.B., Lemon, D.D., Killough, P.M., Hubig, S.M., Atherton, S.J., López­Garriga, J.J., Palmer, G. and Woodruff, W.H. (1993) Photodissociation and recombination of carbonmonoxy cytochrome oxidase: dynamics from picoseconds to kiloseconds. Biochemistry 32, 12013-12024.
  79. Einarsdóttir, Ó., Georgiadis, K.E. and Sucheta, A. (1995) Intramolecular electron transfer and conformational changes in cytochrome c oxidase. Biochemistry 34, 496-508.
  80. Erecinska, M., Wilson, D.F. and Blasie, J.K. (1978a) Studies on the orientations of the mitochondrial redox carriers. I. Orientation of the hemes of cytochrome c oxidase with respect to the plane of a cytochrome oxidase-lipid model membrane. Biochim. Biophys. Acta 501, 53-62.
  81. Erecinska, M., Wilson, D.F. and Blasie, J.K. (1978b) Studies on the orientations of the mitochondrial redox carriers. II. Orientation of the mitochondrial chromophores with respect to the plane of the membrane in hydrated, oriented mitochondrial multilayers. Biochim. Biophys. Acta 501, 63-71.
  82. Espe, M.P., Hosler, J.P., Ferguson­Miller, S., Babcock, G.T. and McCracken, J. (1995) A continuous wave and pulsed EPR characterization of the Mn2+ binding site in Rhodobacter sphaeroides cytochrome c oxidase. Biochemistry 34, 7593-7602.
  83. Fabian, A. and Palmer, G. (1995) The interaction of cytochrome oxidase with hydrogen peroxide: the relationship of compounds P and F. Biochemistry 34, 13802-13810.
  84. Fajer, P., Knowles, P.F. and Marsh, D. (1989) Rotational motion of yeast cytochrome oxidase in phosphatidylcholine complexes studied by saturation­transfer electron spin resonance. Biochemistry 28, 5634-5643.
  85. Fan, C., Bank, J.F., Dorr, R.G. and Scholes, C.P. (1988) An electron nuclear double resonance investigation of redox­induced electronic structural change at CuA2+ in cytochrome c oxidase. J. Biol. Chem. 263, 3588-3591.
  86. Fann, Y.­C., Ahmed, I., Blackburn, N.J., Boswell, J.S., Verkhovskaya, M.L., Hoffman, B.M. and Wikström, M. (1995) Structure of CuB in the binuclear heme-copper center of the cytochrome aa3­type quinol oxidase from Bacillus subtilis: an ENDOR and EXAFS study. Biochemistry 34, 10245-10255.
  87. Farrar, J.A., Thomson, A.J., Cheesman, M.R., Dooley, D.M. and Zumft, W.G. (1991) A model of the copper centres of nitrous oxide reductase (Pseudomonas stutzeri). Evidence from optical, EPR and MCD spectroscopy. FEBS Lett. 294, 11-15.
  88. Farrar, J.A., Lappalainen, P., Zumft, W.G., Saraste, M. and Thomson, A.J. (1995) Spectroscopic and mutagenesis studies on the CuA centre from the cytochrome­c oxidase complex of Paracoccus denitrificans. Eur. J. Biochem. 232, 294-303.
  89. Farrar, J.A., Neese, F., Lappalainen, P., Kroneck, P.M.H., Saraste, M., Zumft, W.G. and Thomson, A.J. (1996) The electronic structure of CuA: A novel mixed­valence dinuclear copper electron­transfer center. J. Am. Chem. Soc. 118, 11501-11514.
  90. Farrar, J.A., Zumft, W.G. and Thomson, A.J. (1998) CuA and CuZ are variants of the electron transfer center in nitrous oxide reductase. Proc. Natl. Acad. Sci. USA 77, 9891-9896.
  91. Fee, J.A., Choc, M.G., Findling, K.L., Lorence, R. and Yoshida, T. (1980) Properties of a copper­containing cytochrome c1aa3 complex: a terminal oxidase of the extreme thermophile Thermus thermophilus HB8. Proc. Natl. Acad. Sci. USA 77, 147-151.
  92. Fee, J.A., Antholine, W.E., Fan, C., Gurbiel, R.J., Surerus, K., Werst, M. and Hoffman, B.M. (1993) Cytochrome c oxidase: A brief introduction and some new results from high field ENDOR studies of the CuA and CuB sites. In Karlin, K.D and Tyeklár, Z., Eds. Bioinorganic Chemistry of Copper. Chapman & Hall, New York, pp. 485-500.
  93. Felsch, J.S., Horvath, M.P., Gursky, S., Hobaugh, M.R., Goudreau, P.N., Fee, J.A., Morgan, W.T., Admiraal, S.J., Ikeda­Saito, M., Fujiwara, T., Fukumori, Y., Yamanaka, T. and Copeland, R.A. (1994) Probing protein-cofactor interactions in the terminal oxidases by second derivative spectroscopy: Study of bacterial enzymes with cofactor substitutions and heme A model compounds. Protein Science 3, 2097-2103.
  94. Fetter, J.R., Qian, J., Shapleigh, J., Thomas, J.W., García­Horsman, A., Schmidt, E., Hosler, J., Babcock, G.T. and Gennis, R.B. (1995) Possible proton relay pathways in cytochrome c oxidase. Proc. Natl. Acad. Sci. USA 92, 1604-1608.
  95. Fiamingo, F.G., Altschuld, R.A., Moh, P.P. and Alben, J.O. (1982) Dynamic interactions of CO with a3Fe and CuB in cytochrome c oxidase in beef heart mitochondria studied by Fourier transform infrared spectroscopy at low temperatures. J. Biol. Chem. 257, 1639-1650.
  96. Fiamingo, F.G., Altschuld, R.A. and Alben, J.O. (1986) alpha and ß forms of cytochrome c oxidase observed in rat heart myocytes by low temperature Fourier transform infrared spectroscopy. J. Biol. Chem. 261, 12976-12987.
  97. Fiamingo, F.G., Jung, D.W. and Alben, J.O. (1990) Structural perturbation of the a3-CuB site in mitochondrial cytochrome c oxidase by alcohol solvents. Biochemistry 29, 4627-4633.
  98. Frey, T.G. and Murray, J.M. (1994) Electron microscopy of cytochrome c oxidase crystals. Monomer­dimer relationship and cytochrome c binding site. J. Mol. Biol. 237, 275-297.
  99. Frey, T.G., Costello, M.J., Karlsson, B., Haselgrove, J.C. and Leigh, J.S. (1982) Structure of the cytochrome c oxidase dimer. Electron microscopy of two­dimensional crystals. J. Mol. Biol. 162, 113-130.
  100. Fry, I.V. and Peschek, G.A. (1988) Electron paramagnetic resonance­detectable Cu2+ in Synechococcus 6301 and 6311: aa3­type cytochrome­c oxidase of cytoplasmic membrane. Methods Enzymol. 167, 450-459.
  101. Fuller, S.D., Capaldi, R.A. and Henderson, R. (1979) Structure of cytochrome c oxidase in deoxycholate­drived two­dimensional crystals. J. Mol. Biol. 134, 305-327.
  102. Fuller, S.D., Capaldi, R.A. and Henderson, R. (1982) Preparation of two­dimensional arrays from purified beef heart cytochrome c oxidase. Biochemistry 21, 2525-2529.
  103. Gamelin, D.R., Randall, D.W., Hay, M.T., Houser, R.P., Mulder, T.C., Canters, G.W., de Vries, S., Tolman, W.B., Lu, Y. and Solomon, E.I. (1998) Spectroscopy of mixed­valence CuA­type centers: Ligand­field control of ground­state properties related to electron transfer. J. Am. Chem. Soc. 120, 5246-5263.
  104. García­Horsman, J.A., Berry, E., Shapleigh, J.P., Alben, J.O. and Gennis, R.B. (1994) A novel cytochrome c oxidase from Rhodobacter sphaeroides that lacks CuA. Biochemistry 33, 3113-3119.
  105. Gelles, J. and Chan, S.I. (1985) Chemical modification of the CuA center in cytochrome c oxidase by sodium p­(hydroxymercuri)benzoate. Biochemistry 24, 3963-3972.
  106. Ghosh, A. and Skancke, A. (1998) Revisiting the putative ferryl tilting mode of oxidized cytochrome c oxidase with density functional vibrational analyses of model complexes. J. Phys. Chem. B102, 10087-10090. Computation
  107. Goodman, G. and Leigh, J.S. (1985) Distance between the visible copper and cytochrome a in bovine heart cytochrome oxidase. Biochemistry 24, 2310-2317.
  108. Goodman, G. and Leigh, J.S. (1987) The distance between cytochromes a and a3 in the azide compound of bovine­heart cytochrome oxidase. Biochim. Biophys. Acta 890, 360-367.
  109. Hallén, S., Brzezinski, P. and Malmström, B.G. (1994) Internal electron transfer in cytochrome c oxidase is coupled to the protonation of a group close to the bimetallic site. Biochemistry 33, 1467-1472.
  110. Haltia, T., Semo, N., Arrondo, J.L., Goni, F.M. and Freire, E. (1994) Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans. Biochemistry 33, 9731-9740.
  111. Han, S., Ching, Y.­C. and Rousseau, D.L. (1989) Evidence for a hydroxide intermediate in cytochrome c oxidase. J. Biol. Chem. 264, 6604-6607.
  112. Han, S., Ching, Y.­C. and Rousseau, D.L. (1990a) Primary intermediate in the reaction of oxygen with fully reduced cytochrome c oxidase. Proc. Natl. Acad. Sci. USA 87, 2491-2495.
  113. Han, S., Ching, Y.­C. and Rousseau, D.L. (1990b) Primary intermediate in the reaction of mixed­valence cytochrome c oxidase with oxygen. Biochemistry 29, 1380-1384.
  114. Han, S., Ching, Y.­C. and Rousseau, D.L. (1990c) Ferryl and hydroxy intermediates in the reaction of oxygen with reduced cytochrome c oxidase. Nature 348, 89-90.
  115. Han, S., Ching, Y.­C. and Rousseau, D.L. (1990d) Cytochrome c oxidase: decay of the primary oxygen intermediate involves direct electron transfer from cytochrome a. Proc. Natl. Acad. Sci. USA 87, 8408-8412.
  116. Hansen, A.P., Britt, R.D., Klein, M.P., Bender, C.J. and Babcock, G.T. (1993) ENDOR and ESEEM studies of cytochrome c oxidase: evidence for exchangeable protons at the CuA site. Biochemistry 32, 13718-13724.
  117. Harmon, P.A., Hendler, R.W. and Levin, I.W. (1994) Resonance Raman and optical spectroscopic monitoring of heme a redox states in cytochrome c oxidase during potentiometric titrations. Biochemistry 33, 699-707.
  118. Hartzell, C.R. and Beinert, H. (1974) Components of cytochrome c oxidase detectable by EPR spectroscopy. Biochim. Biophys. Acta 368, 318-338,
  119. Hartzell, C.R. and Beinert, H. (1976) Oxido­reductive titrations of cytochrome c oxidase followed by EPR spectroscopy. Biochim. Biophys. Acta 423, 323-338.
  120. Hartzell, C.R., Hansen, R.E. and Beinert, H. (1973) Electron carriers of cytochrome oxidase detectable by electron paramagnetic resonance and their relationship to those traditionally recognized in this enzyme. Proc. Natl. Acad. Sci. USA 70, 2477-2481.
  121. Hay, M., Richards, J.H. and Lu, Y. (1996) Construction and characterization of an azurin analog for the purple copper site in cytochrome c oxidase. Proc. Natl. Acad. Sci. USA 93, 461-464.
  122. Heibel, G.E., Hildebrandt, P., Ludwig, B., Steinrucke, P., Soulimane, T. and Buse, G. (1993a) Comparative resonance Raman study of cytochrome c oxidase from beef heart and Paracoccus denitrificans. Biochemistry 32, 10866-10877.
  123. Heibel, G.E., Anzenbacher, P., Hildebrandt, P. and Schafer, G. (1993b) Unusual heme structure in cytochrome aa3 from Sulfolobus acidocaldarius: a resonance Raman investigation. Biochemistry 32, 10878-10884.
  124. Hellwig, P., Rost, B., Kaiser, U., Ostermeier, C., Michel, H. and Mantele, W. (1996) Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: direct evidence by FTIR spectroscopy. FEBS Lett. 385, 53-57.
  125. Hellwig, P., Behr, J., Ostermeier, C., Richter, O.­M.H., Pfitzner, U., Odenwald, A., Ludwig, B., Michel, H. and Mäntele, W. (1998) Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FTIR spectroscopy. Biochemistry 37, 7390-7399.
  126. Hellwig, P., Grzybek, S., Behr, J., Ludwig, B., Michel, H. and Mäntele, W. (1999) Electrochemical and ultraviolet/visible/infrared spectroscopic analysis of heme a and a3 redox reactions in the cytochrome c oxidase from Paracoccus denitrificans: Separation of heme a and a3 contributions and assignment of vibrational modes. Biochemistry 38, 1685-1694.
  127. Henderson, R., Capaldi, R.A. and Leigh, J.S. (1977) Arrangement of cytochrome oxidase molecules in two­dimensional vesicle crystals. J. Mol. Biol. 112, 631-648.
  128. Henkel, G., Müller, A., Weissgräber, S., Buse, G., Soulimane, T., Steffens, G.C.M. and Nolting, H.­F. (1995) The active sites of the native cytochrome­c oxidase from bovine heart mitochondria: EXAFS­spectroscopic characterization of a novel homobinuclear copper center (CuA) and of the heterobinuclear Fea3-CuB center. Angew. Chem. Int. Ed. Engl. 34, 1488-1492.
  129. Hildebrandt, P., Heimburg, T., Marsh, D. and Powell, G.L. (1990) Conformational changes in cytochrome c and cytochrome oxidase upon complex formation: a resonance Raman study. Biochemistry 29, 1661-1668.
  130. Hildebrandt, P., Heibel, G., Anemuller, S. and Schafer, G. (1991) Resonance Raman study of cytochrome aa3 from Sulfolobus acidocaldarius. FEBS Lett. 283, 131-134.
  131. Hildebrandt, P., Vanhecke, F., Buse, G., Soulimane, T. and Mauk, A.G. (1993) Resonance Raman study of the interactions between cytochrome c variants and cytochrome c oxidase. Biochemistry 32, 10912-10922.
  132. Hill, B.C., Brittain, T., Eglinton, D.G., Gadsby, P.M., Greenwood, C., Nicholls, P., Peterson, J., Thomson, A.J. and Woon, T.C. (1983) Low­spin ferric forms of cytochrome a3 in mixed­ligand and partially reduced cyanide­bound derivatives of cytochrome c oxidase. Biochem. J. 215, 57-66.
  133. Hill, B.C., Woon, T.C., Nicholls, P., Peterson, J., Greenwood, C. and Thomson, A.J. (1984) Interactions of sulphide and other ligands with cytochrome c oxidase. An electron­paramagnetic­resonance study. Biochem. J. 224, 591-600.
  134. Hoffman, B.M., Roberts, J.E., Swanson, M., Speck, S.H. and Margoliash, E. (1980) Copper electron­nuclear double resonance of cytochrome c oxidase. Proc. Natl. Acad. Sci. USA 77, 1452-1456.
  135. Holm, D.E., Godette, G., Bonaventura, J., Bonaventura, C. and Peterson, J. (1995) The site of the redox­linked proton pump in eukaryotic cytochrome c oxidases. FEBS Lett. 370, 53-58.
  136. Holm, D.E., Godette, G., Bonaventura, J., Bonaventura, C., Boatright, M.D., Pearce, L.L. and Peterson, J. (1996) A carbon monoxide irreducible form of cytochrome c oxidase and other unusual properties of the "monomeric" shark enzyme. Comp. Biochem. Physiol. B 114, 345-352.
  137. Hosler, J.P., Fetter, J., Tecklenburg, M.M.J., Espe, M.P., Lerma, C. and Ferguson­Miller, S. (1992) Cytochrome aa3 of Rhodobacter sphaeroides as a model for mitochondrial cytochrome c oxidase. Purification, kinetics, proton pumping, and spectral analysis. J. Biol. Chem. 267, 24264-24272.
  138. Hosler, J.P., Shapleigh, J.P., Tecklenburg, M.M.J. Thomas, J.W., Kim, Y., Espe, M.P., Fetter, J., Babcock, G.T., Alben, J.O., Gennis, R.B. and Ferguson­Miller, S. (1994) A loop between transmembrane helices IX and X of subunit I of cytochrome c oxidase caps the heme a-heme a3-CuB center. Biochemistry 33, 1194-1201.
  139. Hosler, J.P., Espe, M.P., Zhen, Y., Babcock, G.T. and Ferguson­Miller, S. (1995) Analysis of site­directed mutants locates a non­redox­active metal near the active site of cytochrome c oxidase of Rhodobacter sphaeroides. Biochemistry 34, 7586-7592.
  140. Hu, V.W., Chan, S.I. and Brown, G.S. (1977) X­ray absorption edge studies on oxidized and reduced cytochrome c oxidase. Proc. Natl. Acad. Sci. USA 74, 3821-3825.
  141. Ishibe, N., Lynch, S.R. and Copeland, R.A. (1991) The pH dependence of cytochrome a conformation in cytochrome c oxidase. J. Biol. Chem. 266, 23916-23920.
  142. Iwase, T., Varotsis, C., Shinzawa­Itoh, K., Yoshikawa, S. and Kitagawa, T. (1999) Infrared evidence for CuB ligation of photodissociated CO of cytochrome c oxidase at ambient temperatures and accompanied deprotonation of a carboxyl side chain of protein. J. Am. Chem. Soc. 121, 1415-1416.
  143. Iwata, S., Ostermeier, C., Ludwig, B. and Michel, H. (1995) Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376, 660-669.
  144. Johnson, M.K., Eglinton, D.G., Gooding, P.E., Greenwood, C. and Thomson, A.J. (1981) Characterization of the partially reduced cyanide­inhibited derivative of cytochrome c oxidase by optical, electron­paramagnetic­resonance and magnetic­circular­dichroism spectroscopy. Biochem. J. 193, 699-708.
  145. Kai, M., Yano, T., Tamegai, H., Fukumori, Y. and Yamanaka, T. (1992) Thiobacillus ferrooxidans cytochrome c oxidase: purification, and molecular and enzymatic features. J. Biochem. (Tokyo) 112, 816-821.
  146. Kannt, A., Lancaster, C.R.D. and Michel, H. (1998) The coupling of electron transfer and proton translocation: Electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase. Biophys. J. 74, 708-721. Computation
  147. Karlin, S., Zhu, Z.­Y. and Karlin, K.D. (1998) Extended metal environments of cytochrome c oxidase structures. Biochemistry 37, 17726-17734.
  148. Karlsson, B. and Andréasson, L.­E. (1981) The identity of a new copper(II) electron paramagnetic resonance signal in cytochrome c oxidase. Biochim. Biophys. Acta 635, 73-80.
  149. Kauffman, K.E., Goddard, C.A., Zang, Y., Holm, R.H. and Münck, E. (1997) Mössbauer and magnetization studies of heme-copper­bridged assemblies pertinent to cytochrome c oxidase. Inorg. Chem. 36, 985-993.
  150. Kent, T.A., Münck, E., Dunham, W.R., Filter, W.F., Findling, K.L., Yoshida, T.A. and Fee, J.A. (1982) Mössbauer study of a bacterial cytochrome oxidase: cytochrome c1aa3 from Thermus thermophilus. J. Biol. Chem. 257, 12489-12492.
  151. Kent, T.A., Young, L.J., Palmer, G., Fee, J.A. and Münck, E. (1983) Mössbauer study of beef heart cytochrome oxidase. Comparative study of the bovine enzyme and cytochrome c1aa3 from Thermus thermophilus. J. Biol. Chem. 258, 8543-8546.
  152. Kim, Y., Babcock, G.T., Surerus, K.K., Fee, J.A., Dyer, R.B., Woodruff, W.H. and Oertling, W.A. (1998) Cyanide binding and active site structure in heme-copper oxidases: Normal coordinate analysis of iron-cyanide vibrations of a32+CN¯ complexes of cytochromes ba3 and aa3. Biospectroscopy 4, 1-15.
  153. Kitagawa, T. and Orii, Y. (1978) Resonance Raman studies of cytochrome oxidase. J. Biochem. (Tokyo) 84, 1245-1252.
  154. Kobayashi, K., Une, H. and Hayashi, K. (1989) Electron transfer process in cytochrome oxidase after pulse radiolysis. J. Biol. Chem. 264, 7976-7980.
  155. Kojima, N. and Palmer, G. (1983) Further characterization of the potentiometric behavior of cytochrome oxidase. Cytochrome alpha stays low spin during oxidation and reduction. J. Biol. Chem. 258, 14908-14913.
  156. Konstantinov, A.A., Siletsky, S., Mitchell, D., Kaulen, A. and Gennis, R.B. (1997) The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site­directed mutations on time­resolved electrogenic intraprotein proton transfer. Proc. Natl. Acad. Sci. USA 94, 9085-9090.
  157. Kroneck, P.M.H., Antholine, W.E., Riester, J. and Zumft, W.G. (1988) The cupric site in nitrous oxide reductase contains a mixed­valence [Cu(II),Cu(I)] binuclear center: a multifrequency electron paramagnetic resonance investigation. FEBS Lett. 242, 70-74.
  158. Kroneck, P.M.H., Antholine, W.E., Kastrau, D.H.W., Buse, G., Steffens, G.C. and Zumft, W.G. (1990) Multifrequency EPR evidence for a bimetallic center at the CuA site in cytochrome c oxidase. FEBS Lett. 268, 274-276.
  159. Kroneck, P.M.H., Antholine, W.E., Koteich, H., Kastrau, D.H.W., Neese, F. and Zumft, W.G. (1993) The EPR­detectable copper of nitrous oxide reductase as a model for CuA in cytochrome c oxidase: A multifrequency electron paramagnetic resonance investigation. In Karlin, K.D and Tyeklár, Z., Eds. Bioinorganic Chemistry of Copper. Chapman & Hall, New York, pp. 419-426.
  160. Lappalainen, P., Aasa, R., Malmström, B.G. and Saraste, M. (1993) Soluble CuA­binding domain from the Paracoccus cytochrome c oxidase. J. Biol. Chem. 268, 26416-26421.
  161. Larsen, R.W., Ondrias, M.R., Copeland, R.A., Li, P.M. and Chan, S.I. (1989) Resonance Raman studies of CuA­modified cytochrome c oxidase. Biochemistry 28, 6418-6422.
  162. Larsen, R.W., Li, W., Copeland, R.A., Witt, S.N., Lou, B.S., Chan, S.I. and Ondrias, M.R. (1990) Room temperature characterization of the dioxygen intermediates of cytochrome c oxidase by resonance Raman spectroscopy. Biochemistry 29, 10135-10140.
  163. Larsson, S., Kallebring, B., Wittung, P. and Malmström, B.G. (1995) The CuA center of cytochrome­c oxidase: electronic structure and spectra of models compared to the properties of CuA domains. Proc. Natl. Acad. Sci. USA 92, 7167-7171.
  164. Lauraeus, M., Wikström, M., Varotsis, C., Tecklenburg, M.M.J. and Babcock, G.T. (1992) Optical and resonance Raman spectroscopy of the heme groups of the quinol­oxidizing cytochrome aa3 of Bacillus subtilis. Biochemistry 31, 10054-10060.
  165. Li, P.M., Gelles, J., Chan, S.I., Sullivan, R.J. and Scott, R.A. (1987) Extended X­ray absorption fine structure of copper in CuA­depleted, p­(hydroxymercuri)benzoate­modified, and native cytochrome c oxidase. Biochemistry 26, 2091-2095.
  166. Li, P.M., Morgan, J.E., Nilsson, T., Ma, M. and Chan, S.I. (1988) Heat treatment of cytochrome c oxidase perturbs the CuA site and affects proton pumping behavior. Biochemistry 27, 7538-7546.
  167. Li, W. and Palmer, G. (1993) Spectroscopic characterization of the interaction of azide and thiocyanate with the binuclear center of cytochrome oxidase: evidence for multiple ligand sites. Biochemistry 32, 1833-1843.
  168. Liao, G.­L. and Palmer, G. (1998) Diazene - A not so innocent ligand for the binuclear center of cytochrome c oxidase. Biochemistry 37, 15583-15592.
  169. LoBrutto, R., Wei, Y.H., Mascarenhas, R., Scholes, C.P. and King, T.E. (1983) Electron nuclear double resonance and electron paramagnetic resonance study on the structure of the NO­ligated heme alpha3 in cytochrome c oxidase. J. Biol. Chem. 258, 7437-7448.
  170. Luchinat, C., Soriano, A., Djinovic­Carugo,K., Saraste, M., Malmström, B.G. and Bertini, I. (1997) Electronic and geometric structure of the CuA site studied by 1H NMR in a soluble domain of cytochrome c oxidase from Paracoccus denitrificans. J. Am. Chem. Soc. 119, 11023-11027.
  171. Lynch, S.R., Carter, R.H. and Copeland, R.A. (1993) Resonance Raman spectroscopy of the cytochrome c oxidase from Paracoccus denitrificans. Biochemistry 32, 6923-6927.
  172. Martin, C.T., Scholes, C.P. and Chan, S.I. (1985) The identification of histidine ligands to cytochrome a in cytochrome c oxidase. J. Biol. Chem. 260, 2857-2861.
  173. Martin, C.T., Scholes, C.P. and Chan, S.I. (1988) On the nature of cysteine coordination to CuA in cytochrome c oxidase. J. Biol. Chem. 263, 8420-8429.
  174. Mims, W.B., Peisach, J., Shaw, R.W. and Beinert, H. (1980) Electron spin echo studies of cytochrome c oxidase. J. Biol. Chem. 255, 6843-6846.
  175. Mitchell, D.M., Aasa, R., Ädelroth, P., Brzezinski, P., Gennis, R.B. and Malmström, B.G. (1995) EPR studies of wild­type and several mutants of cytochrome c oxidase from Rhodobacter sphaeroides: Glu286 is not a bridging ligand in the cytochrome a3-CuB center. FEBS Lett. 374, 371-374.
  176. Mitchell, D.M., Ädelroth, P., Hosler, J.P., Fetter, J.R., Brzezinski, P., Pressler, M.A., Aasa, R., Malmström, B.G., Alben, J.O., Babcock, G.T., Gennis, R.B. and Ferguson­Miller, S. (1996a) A ligand­exchange mechanism of proton pumping involving tyrosine­422 of subunit I of cytochrome oxidase is ruled out. Biochemistry 35, 824-828.
  177. Mitchell, D.M., Shapleigh, J.P., Archer, A.M., Alben, J.O. and Gennis, R.B. (1996b) A pH­dependent polarity change at the binuclear center of reduced cytochrome c oxidase detected by FTIR difference spectroscopy of the CO adduct. Biochemistry 35, 9446-9450.
  178. Mitchell, R., Mitchell, P. and Rich, P.R. (1991) The assignment of the 655 nm spectral band of cytochrome oxidase. FEBS Lett. 280, 321-324.
  179. Moënne­Loccoz, P. and de Vries, S. (1998) Structural characterization of the catalytic high­spin heme b of nitric oxide reductase: A resonance Raman study. J. Am. Chem. Soc. 120, 5147-5152.
  180. Moody, A.J., von Germar, F., Mantele, W. and Rich, P.R. (1995) Rapid­scan FTIR spectroscopic studies on the photolysis and recombination of the cyanide adduct of fully reduced bovine cytochrome c oxidase. Biochem. Soc. Trans. 23, 521S.
  181. Moss, T.H., Shapiro, E., King, T.E., Beinert, H. and Hartzell, C. (1978) The magnetic susceptibility of cytochrome oxidase in the 4.2-1.5 K range. J. Biol. Chem. 253, 8072-8073.
  182. Muhoberac, B.B. and Wharton, D.C. (1983) Electron paramagnetic resonance study of the interaction of some anionic ligands with oxidized Pseudomonas cytochrome oxidase. J. Biol. Chem. 258, 3019-3027.
  183. Musatov, A. and Konstantinov, A.A. (1988) Conformational change of cytochrome a3 induced by oxidized cytochrome c. FEBS Lett. 238, 295-299.
  184. Musser, S.M., Larsen, R.W. and Chan, S.I. (1993) Fluorescence quenching of reconstituted NCD­4­labeled cytochrome c oxidase complex by DOXYL­stearic acids. Biophys. J. 65, 2348-2359.
  185. Musser, S.M., Fann, Y.­C., Gurbiel, R.J., Hoffman, B.M. and Chan, S.I. (1997) Q­band electron nuclear double resonance (ENDOR) and X­band EPR of the sulfobetaine 12 heat­treated cytochrome c oxidase complex. J. Biol. Chem. 272, 203-209.
  186. Naqui, A., Kumar, C., Ching, Y.­C., Powers, L. and Chance, B. (1984) Structure and reactivity of multiple forms of cytochrome oxidase as evaluated by X­ray absorption spectroscopy and kinetics of cyanide binding. Biochemistry 23, 6222-6227.
  187. Neese, F., Zumft, W.G., Antholine, W.E. and Kroneck, P.M.H. (1996) The purple mixed­valence CuA center in nitrous­oxide reductase: EPR of the copper­63­, copper­65­, and both copper­65­ and [15N]histidine­enriched enzyme and a molecular orbital interpretation. J. Am. Chem. Soc. 118, 8692-8699.
  188. Neese, F., Kappl, R., Hüttermann, J., Zumft, W.G. and Kroneck, P.M.H. (1998) Probing the ground state of the purple mixed valence CuA center in nitrous oxide reductase: a CW ENDOR (X­band) study of the 65Cu, 15N­histidine labeled enzyme and interpretation of hyperfine couplings by molecular orbital calculations. J. Biol. Inorg. Chem. 3, 53-67.
  189. Nilsson, T., Copeland, R.A., Smith, P.A. and Chan, S.I. (1988) Conversion of CuA to a type II copper in cytochrome c oxidase. Biochemistry 27, 8254-8260.
  190. Oertling, W.A., Surerus, K.K., Einarsdottir, O., Fee, J.A., Dyer, R.B. and and Woodruff, W.H. (1994) Spectroscopic characterization of cytochrome ba3, a terminal oxidase from Thermus thermophilus: comparison of the a3/CuB site to that of bovine cytochrome aa3. Biochemistry 33, 3128-3141.
  191. Oganesyan, V.S., Butler, C.S., Watmough, N.J., Greenwood, C., Thomson, A.J. and Cheesman, M.R. (1998) Nature of the coupling between the high­spin Fe(III) heme and CuB(II) in the active site of terminal oxidases: Dual­mode EPR spectra of fluoride cytochrome bo3. J. Am. Chem. Soc. 120, 4232-4233.
  192. Ogura, T., Sone, N., Tagawa, K. and Kitagawa, T. (1984) Resonance Raman study of the aa3­type cytochrome oxidase of thermophilic bacterium PS3. Biochemistry 23, 2826-2831.
  193. Ogura, T., Yoshikawa, S. and Kitagawa, T. (1985a) Resonance Raman spectra for catalytic intermediates of cytochrome c oxidase detected with a mixed flow transient apparatus. Biochim. Biophys. Acta 832, 220-223.
  194. Ogura, T., Yoshikawa, S. and Kitagawa, T. (1985b) Resonance Raman study on photoreduction of cytochrome c oxidase: distinction of cytochromes a and a3 in the intermediate oxidation states. Biochemistry 24, 7746-7752.
  195. Ogura, T., Yoshikawa, S. and Kitagawa, T. (1989) Raman/absorption simultaneous measurements for cytochrome oxidase compound A at room temperature with a novel flow apparatus. Biochemistry 28, 8022-8027.
  196. Ogura, T., Takahashi, S., Shinzawa­Itoh, K., Yoshikawa, S. and Kitagawa, T. (1990) Observation of the Fe4+=O stretching Raman band for cytochrome oxidase compound B at ambient temperature. J. Biol. Chem. 265, 14721-14723.
  197. Ogura, T., Hirota, S., Proshlyakov, D.A., Shinzawa­Itoh, K., Yoshikawa, S. and Kitagawa, T. (1996) Time­resolved resonance Raman evidence for tight coupling between electron transfer and proton pumping of cytochrome c oxidase upon the change from the FeV oxidation level to the FeIV oxidation level. J. Am. Chem. Soc. 118, 5443-5449.
  198. Ohnishi, T., Harmon, H.J. and Waring, A.J. (1985) Electron­paramagnetic­resonance studies on the spatial relationship of redox components in cytochrome oxidase. Biochem. Soc. Trans. 13, 607-611.
  199. Ortwein, C., Link, T.A., Meunier, B., Colson­Corbisier, A.­M., Rich, P.R. and Brandt, U. (1997) Structural and functional analysis of deficient mutants in subunit I of cytochrome c oxidase from Saccharomyces cerevisiae. Biochim. Biophys. Acta 1321, 79-92.
  200. Ostermeier, C., Essen, L.O. and Michel, H. (1995a) Crystals of an antibody Fv fragment against an integral membrane protein diffracting to 1.28 Å resolution. Proteins 21, 74-77.
  201. Ostermeier, C., Iwata, S., Ludwig, B. and Michel, H. (1995b) Fv fragment­mediated crystallization of the membrane protein bacterial cytochrome c oxidase. Nature Struct. Biol. 2, 842-846.
  202. Ostermeier, C., Harrenga, A., Ermler, U. and Michel, H. (1997) Structure at 2.7 Å resolution of the Paracoccus denitrificans two­subunit cytochrome c oxidase complexed with an antibody Fv fragment. Proc. Natl. Acad. Sci. USA 94, 10547-10553.
  203. Ozawa, T., Suzuki, H. and Tanaka, M. (1980) Crystallization of part of the mitochondrial electron transfer chain: cytochrome c oxidase-cytochrome c complex. Proc. Natl. Acad. Sci. USA 77, 928-930.
  204. Ozawa, T., Tanaka, M. and Wakabayashi, T. (1982) Crystallization of mitochondrial cytochrome oxidase. Proc. Natl. Acad. Sci. USA 79, 7175-7179.
  205. Paddy, M.R., Dahlquist, F.W., Davis, J.H. and Bloom, M. (1981) Dynamical and temperature-dependent effects of lipid­protein interactions. Application of deuterium nuclear magnetic resonance and electron paramagnetic resonance spectroscopy to the same reconstitutions of cytochrome c oxidase. Biochemistry 20, 3152-3162.
  206. Palmer, G., Mackler, B. and Duncan, H.M. (1967) Electron paramagnetic resonance studies on the cytochrome oxidase from yeast. Biochim. Biophys. Acta 143, 636-638.
  207. Palmer, G., Babcock, G.T. and Vickery, L.E. (1976) A model for cytochrome oxidase. Proc. Natl. Acad. Sci. USA 73, 2206-2210.
  208. Paula, S., Sucheta, A., Szundi, I. and Einarsdóttir, Ó. (1999) Proton and electron transfer during the reduction of molecular oxygen by fully reduced cytochrome c oxidase: A flow­flash investigation using optical multichannel detection. Biochemistry 38, 3025-3033.
  209. Peterson, J., Day, E.P., Pearce, L.L. and Wilson, M.T. (1995) Measurement of the spin concentration of metalloprotein samples from saturation­magnetization data with particular reference to cytochrome c oxidase. Biochem. J. 305, 871-878.
  210. Pfitzner, U., Odenwald, A., Ostermann, T., Weingard, L., Ludwig, B. and Richter, O.M. (1998) Cytochrome c oxidase (heme aa3) from Paracoccus denitrificans: Analysis of mutations in putative proton channels of subunit I. J. Bioenerg. Biomembr. 30, 89-97.
  211. Powers, L. and Chance, B. (1985) Multiple structures and functions of cytochrome oxidase. J. Inorg. Biochem. 23, 207-217.
  212. Powers, L. and Kincaid, B.M. (1989) Comparison of the data, analysis, and results of X­ray absorption studies of cytochrome c oxidase. Biochemistry 28, 4461-4468.
  213. Powers, L., Blumberg, W.E., Chance, B., Barlow, C.H., Leigh, J.S., Smith, J., Yonetani, T., Vik, S. and Peisach, J. (1979) The nature of the copper atoms of cytochrome c oxidase as studied by optical and x­ray absorption edge spectroscopy. Biochim. Biophys. Acta 546, 520-538.
  214. Powers, L., Chance, B., Ching, Y.­C., Muhoberac, B., Weintraub, S.T. and Wharton, D.C. (1982) Structural features of the copper­depleted cytochrome oxidase from beef heart: iron EXAFS. FEBS Lett. 138, 245-248.
  215. Powers, L., Chance, B., Ching, Y.­C. and Lee, C.P. (1987) Structure of the copper sites in membrane­bound cytochrome c oxidase. J. Biol. Chem. 262, 3160-3164.
  216. Powers, L., Lauraeus, M., Reddy, K.S., Chance, B. and Wikström, M. (1994) Structure of the binuclear heme iron­copper site in the quinol­oxidizing cytochrome aa3 from Bacillus subtilis. Biochim. Biophys. Acta 1183, 504-512.
  217. Proshlyakov, D.A., Ogura, T., Shinzawa­Itoh, K., Yoshikawa, S., Appelman, E.H. and Kitagawa, T. (1994) Selective resonance Raman observation of the "607 nm" form generated in the reaction of oxidized cytochrome c oxidase with hydrogen peroxide. J. Biol. Chem. 269, 29385-29388.
  218. Proshlyakov, D.A., Ogura, T., Shinzawa­Itoh, K., Yoshikawa, S. and Kitagawa, T. (1996a) Microcirculating system for simultaneous determination of Raman and absorption spectra of enzymatic reaction intermediates and its application to the reaction of cytochrome c oxidase with hydrogen peroxide. Biochemistry 35, 76-82.
  219. Proshlyakov, D.A., Ogura, T., Shinzawa­Itoh, K., Yoshikawa, S. and Kitagawa, T. (1996b) Resonance Raman/absorption characterization of the oxo intermediates of cytochrome c oxidase generated in its reaction with hydrogen peroxide: pH and H2O2 concentration dependence. Biochemistry 35, 8580-8586.
  220. Proshlyakov, D.A., Pressler, M.A. and Babcock, G.T. (1998) Dioxygen activation and bond cleavage by mixed­valence cytochrome c oxidase. Proc. Natl. Acad. Sci. USA 95, 8020-8025.
  221. Qian, J., Shi, W., Pressler, M., Hoganson, C., Mills, D., Babcock, G.T. and Ferguson­Miller, S. (1997) Aspartate­407 in Rhodobacter sphaeroides cytochrome c oxidase is not required for proton pumping or manganese binding. Biochemistry 36, 2539-2543.
  222. Ray, G.B., Copeland, R.A., Lee, C.P. and Spiro, T.G. (1990) Resonance Raman evidence for low­spin Fe2+ heme a3 in energized cytochrome c oxidase: implications for the inhibition of O2 reduction. Biochemistry 29, 3208-3213.
  223. Reinhammar, B., Malkin, R., Jensen, P., Karlsson, B., Andréasson, L.­E., Aasa, R., Vänngård, T. and Malmström, B.G. (1980) A new copper(II) electron paramagnetic resonance signal in two laccases and in cytochrome c oxidase. J. Biol. Chem. 255, 5000-5003.
  224. Rich, P.R., Moody, A.J. and Ingledew, W.J. (1992) Detection of a near infra­red absorption band of ferrohaem a3 in cytochrome c oxidase. FEBS Lett. 305, 171-173.
  225. Richaud, P. and Denis, M. (1984) A near­infrared investigation of cytochrome c oxidase in higher plant mitochondria. Arch. Biochem. Biophys. 232, 8-16.
  226. Rosen, S. (1978) Kinetic studies on oxidized and partially reduced cytochrome c oxidase. Biochim. Biophys. Acta 503, 389-397.
  227. Rousseau, D.L., Singh, S., Ching, Y.­C. and Sassaroli, M. (1988a) Nitrosyl cytochrome c oxidase. Formation and properties of mixed valence enzyme. J. Biol. Chem. 263, 5681-5685.
  228. Rousseau, D.L., Sassaroli, M., Ching, Y.­C. and Dasgupta, S. (1988b) The role of water near cytochrome a in cytochrome c oxidase. Ann. N. Y. Acad. Sci. 550, 223-237.
  229. Salgado, J., Warmerdam, G., Bubacco, L. and Canters, G.W. (1998) Understanding the electronic properties of the CuA site from the soluble domain of cytochrome c oxidase through paramagnetic 1H NMR. Biochemistry 37, 7378-7389.
  230. Salmeen, I., Rimai, L., Gill, D., Yamamoto, T., Palmer, G., Hartzell, C.R. and Beinert, H. (1973) Resonance Raman spectroscopy of cytochrome c oxidase and electron transport particles with excitation near the Soret band. Biochem. Biophys. Res. Commun. 52, 1100-1107.
  231. Salmeen, I., Rimai, L. and Babcock, G. (1978) Raman spectra of heme a, cytochrome oxidase-ligand complexes, and alkaline denatured oxidase. Biochemistry 17, 800-806.
  232. Sassaroli, M., Ching, Y.­C., Argade, P.V. and Rousseau, D.L. (1988) Photodissociated cytochrome c oxidase: cryotrapped metastable intermediates. Biochemistry 27, 2496-2502.
  233. Sassaroli, M., Ching, Y.­C., Dasgupta, S. and Rousseau, D.L. (1989) Cytochrome c oxidase: evidence for interaction of water molecules with cytochrome a. Biochemistry 28, 3128-3132.
  234. Schoonover, J.R. and Palmer, G. (1991) Reaction of formate with the fast form of cytochrome oxidase: a model for the fast to slow conversion. Biochemistry 30, 7541-7550.
  235. Schoonover, J.R., Dyer, R.B., Woodruff, W.H., Baker, G.M., Noguchi, M. and Palmer, G. (1988) A comparison of the resonance Raman properties of the fast and slow forms of cytochrome oxidase. Biochemistry 27, 5433-5440.
  236. Scott, R.A., Schwartz, J.R. and Cramer, S.P. (1985) Effect of cyanide binding on the copper sites of cytochrome c oxidase: An X­ray absorption spectroscopic study. J. Inorg. Biochem. 23, 199-205.
  237. Scott, R.A., Schwartz, J.R. and Cramer, S.P. (1986) Structural aspects of the copper sites in cytochrome c oxidase. An X­ray absorption spectroscopic investigation of the resting­state enzyme. Biochemistry 25, 5546-5555.
  238. Scott, R.A., Zumft, W.G., Coyle, C.L. and Dooley, D.M. (1989) Pseudomonas stutzeri N2O reductase contains CuA­type sites. Proc. Natl. Acad. Sci. USA 86, 4082-4086.
  239. Seelig, A. and Seelig, J. (1985) Phospholipid composition and organization of cytochrome c oxidase preparations as determined by 31P­nuclear magnetic resonance. Biochim. Biophys. Acta 815, 153-158.
  240. Seelig, A., Ludwig, B., Seelig, J. and Schatz, G. (1981) Copper and manganese electron spin resonance studies of cytochrome c oxidase from Paracoccus denitrificans. Biochim. Biophys. Acta 636, 162-167.
  241. Seiter, C.H. and Angelos, S.G. (1980) Cytochrome oxidase: an alternative model. Proc. Natl. Acad. Sci. USA 77, 1806-1808.
  242. Shapleigh, J.P., Hill, J.J., Alben, J.O. and Gennis, R.B. (1992a) Spectroscopic and genetic evidence for two heme-Cu­containing oxidases in Rhodobacter sphaeroides. J. Bacteriol. 174, 2338-2343.
  243. Shapleigh, J.P., Hosler, J.P., Tecklenburg, M.M.G., Kim, Y., Babcock, G.T., Gennis, R.B. and Ferguson­Miller, S. (1992b) Definition of the catalytic site of cytochrome c oxidase: specific ligands of heme a and the heme a3-CuB center. Proc. Natl. Acad. Sci. USA 89, 4786-4790.
  244. Sharonov, Yu.A., Sharonova, N.A., Figlovsky, V.A. and Grigorjev, V.A. (1982) A comparison of the heme electronic states in equilibrium and nonequilibrium protein conformations of high­spin ferrous hemoproteins. Low temperature magnetic circular dichroism studies. Biochim. Biophys. Acta 709, 332-341.
  245. Shaw, R.W., Hansen, R.E. and Beinert, H. (1978a) A novel electron paramagnetic resonance signal of "oxygenated" cytochrome c oxidase. J. Biol. Chem. 253, 6637-6640.
  246. Shaw, R.W., Hansen, R.E. and Beinert, H. (1978b) Responses of the a3 component of cytochrome c oxidase to substrate and ligand addition. Biochim. Biophys. Acta 504, 187-199.
  247. Shinzawa­Itoh, K., Yamashita, H., Yoshikawa, S., Fukumoto, Y., Abe, T. and Tsukihara, T. (1992) Single crystals of bovine heart cytochrome c oxidase at fully oxidized resting, fully reduced and CO­bound fully reduced states are isomorphous with each other. J. Mol. Biol. 228, 987-990.
  248. Shinzawa­Itoh, K., Ueda, H., Yoshikawa, S., Aoyama, H., Yamashita, E. and Tsukihara, T. (1995) Effects of ethyleneglycol chain length of dodecyl polyethyleneglycol monoether on the crystallization of bovine heart cytochrome c oxidase. J. Mol. Biol. 246, 572-575.
  249. Slutter, C.E., Sanders, D., Wittung, P., Malmström, B.G., Aasa, R., Richards, J.H., Gray, H.B. and Fee, J.A. (1996) Water­soluble, recombinant CuA­domain of the cytochrome ba3 subunit II from Thermus thermophilus. Biochemistry 35, 3387-3395.
  250. Sone, N., Ogura, T. and Kitagawa, T. (1986) Iron­histidine stretching Raman line and enzymic activities of bovine and bacterial cytochrome c oxidases. Biochim. Biophys. Acta 850, 139-145.
  251. Soulimane, T. and Buse, G. (1995) Integral cytochrome­c oxidase. Preparation and progress towards a three­dimensional crystallization. Eur. J. Biochem. 227, 588-595.
  252. Stevens, T.H., Brudvig, G.W., Bocian, D.F. and Chan, S.I. (1979) Structure of cytochrome a3-Cua3 couple in cytochrome c oxidase as revealed by nitric oxide binding studies. Proc. Natl. Acad. Sci. USA 76, 3320-3324.
  253. Stevens, T.H., Martin, C.T., Wang, H., Brudvig, G.W., Scholes, C.P. and Chan, S.I. (1982) The nature of CuA in cytochrome c oxidase. J. Biol. Chem. 257, 12106-12113.
  254. Sucheta, A., Szundi, I. and Einarsdóttir, Ó. (1998) Intermediates in the reaction of fully reduced cytochrome c oxidase with dioxygen. Biochemistry 37, 17905-17914.
  255. Takahashi, S., Ogura, T., Shinzawa­Itoh, K., Yoshikawa, S. and Kitagawa, T. (1993) Resonance Raman studies on the CuA site of cytochrome c oxidase using a multichannel scanning Raman spectrometer with a CCD detector. Biochemistry 32, 3664-3670.
  256. Takahashi, S., Ching, Y.­C., Wang, J. and Rousseau, D.L. (1995) Microsecond generation of oxygen­bound cytochrome c oxidase by rapid solution mixing. J. Biol. Chem. 270, 8405-8407.
  257. Takano, T., Dickerson, R.E., Schichman, S.A. and Meyer, T.E. (1979) Crystal data, molecular dimensions and molecular symmetry in cytochrome oxidase from Pseudomonas aeruginosa. J. Mol. Biol. 133, 185-188.
  258. Tanaka, M., Suzuki, H. and Ozawa, T. (1980) The crystallization of mitochondrial cytochrome oxidase-cytochrome c complex. Biochim. Biophys. Acta 612, 295-298.
  259. Thomson, A.J., Brittain, T., Greenwood, C. and Springall, J.P. (1977) Variable­temperature magnetic­circular­dichroism spectra of cytochrome c oxidase and its derivatives. Biochem. J. 165, 327-336.
  260. Thomson, A.J., Johnson, M.K., Greenwood, C. and Gooding, P.E. (1981) A study of the magnetic properties of haem a3 in cytochrome c oxidase by using magnetic­circular­dichroism spectroscopy. Biochem. J. 193, 687-697.
  261. Thomson, A.J., Englinton, D.G., Hill, B.C. and Greenwood, C. (1982) The nature of haem a3 in the oxidized state of cytochrome c oxidase. Evidence from low­temperature magnetic­circular­dichroism spectroscopy in the near infrared region. Biochem. J. 207, 167-170.
  262. Tihova, M., Tattrie, B. and Nicholls, P. (1993) Electron microscopy of cytochrome c oxidase­containing proteoliposomes: imaging analysis of protein orientation and monomer­dimer behaviour. Biochem. J. 292, 933-946.
  263. Tomizaki, T., Yamashita, E., Yamaguchi, H., Aoyama, H., Tsukihara, T., Shinzawa­Itoh, K., Nakashima, R., Yaono, R. and Yoshikawa, S. (1999) Structure analysis of bovine heart cytochrome c oxidase at 2.8 Å resolution. Acta Crystallogr. D55, 31-45.
  264. Tsubaki, M. (1993a) Fourier­transform infrared study of cyanide binding to the Fea3-CuB binuclear site of bovine heart cytochrome c oxidase: Implication of the redox­linked conformational change at the binuclear site. Biochemistry 32, 164-173.
  265. Tsubaki, M. (1993b) Fourier­transform infrared study of azide binding to the Fea3-CuB binuclear site of bovine heart cytochrome c oxidase: New evidence for a redox­linked conformational change at the binuclear site. Biochemistry 32, 174-182.
  266. Tsukihara, T., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa­Itoh, K., Nakashima, R., Yaono, R. and Yoshikawa, S. (1995) Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 Å. Science 269, 1069-1074.
  267. Tsukihara, T., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa­Itoh, K., Nakashima, R., Yaono, R. and Yoshikawa, S. (1996a) Crystal structure of bovine heart cytochrome c oxidase at 2.8 Å resolution. Folding & Design 1, A164.
  268. Tsukihara, T., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa­Itoh, K., Nakashima, R., Yaono, R. and Yoshikawa, S. (1996b) The whole structure of the 13­subunit oxidized cytochrome c oxidase at 2.8 Å. Science 272, 1136-1144.
  269. Tuzi, S., Shinzawa­Itoh, K., Erata, T., Naito, A., Yoshikawa, S. and Saito, H. (1992) A high­resolution solid­state 13C­NMR study on crystalline bovine heart cytochrome­c oxidase and lysozyme. Dynamic behavior of protein and detergent in the complex. Eur. J. Biochem. 208, 713-720.
  270. Tweedle, M.F. and Wilson, L.J. (1978) Electronic state of heme in cytochrome oxidase. III. The magnetic susceptibility of beef heart cytochrome oxidase and some of its derivatives from 7-200 K. Direct evidence for an antiferromagnetically coupled Fe(III)/Cu(II) pair. J. Biol. Chem. 253, 8065-8071.
  271. Valpuesta, J.M., Henderson, R. and Frey, T.G. (1990) Electron cryo­microscopic analysis of crystalline cytochrome oxidase. J. Mol. Biol. 214, 237-251.
  272. Vamvouka, M., Müller, W., Ludwig, B. and Varotsis, C. (1999) Fourier transform infrared and resonance Raman studies of the interaction of azide with cytochrome c oxidase from Paracoccus denitrificans. J. Phys. Chem. B103, 3030-3034.
  273. van Camp, H.L., Wei, Y.H., Scholes, C.P. and King, T.E. (1978) Electron nuclear double resonance of cytochrome oxidase: nitrogen and proton ENDOR from the `copper' EPR signal. Biochim. Biophys. Acta 537, 238-246.
  274. van Gelder, B.F., Orme­Johnson, W.H., Hansen, R.E., and Beinert, H. (1967) Electron paramagnetic resonance of heme at intermediate oxidation states of cytochrome c oxidase. Proc. Natl. Acad. Sci. USA 58, 1073-1079.
  275. Vänngård, T. (1985) Electron­paramagnetic­resonance studies of structure and function of the two­haem enzymes Pseudomonas cytochrome c peroxidase and beef heart cytochrome c oxidase. Biochem. Soc. Trans. 13, 619-622.
  276. Varotsis, C. and Babcock, G.T. (1990) Appearance of the v(FeIV=O) vibration from a ferryl­oxo intermediate in the cytochrome oxidase/dioxygen reaction. Biochemistry 29, 7357-7362.
  277. Varotsis, C. and Vamvouka, M. (1998) Resonance Raman and FTIR studies of carbon monoxide­bound cytochrome aa3­600 oxidase of Bacillus subtilis. J. Phys. Chem. B102, 7670-7673.
  278. Varotsis, C., Woodruff, W.H. and Babcock, G.T. (1990) Direct detection of a dioxygen adduct of cytochrome a3 in the mixed valence cytochrome oxidase/dioxygen reaction. J. Biol. Chem. 265, 11131-11136.
  279. Varotsis, C., Zhang, Y., Appelman, E.H. and Babcock, G.T. (1993) Resolution of the reaction sequence during the reduction of O2 by cytochrome oxidase. Proc. Natl. Acad. Sci. USA 90, 237-241.
  280. Volpe, J.A., O'Toole, M.C. and Caughey, W.S. (1975) Quantitative infrared spectroscopy of CO complexes of cytochrome c oxidase, hemoglobin and myoglobin: evidence for one CO per heme. Biochem. Biophys. Res. Commun. 62, 48-53.
  281. von Wachenfeldt, C., de Vries, S. and van der Oost J. (1994) The CuA site of the caa3­type oxidase of Bacillus subtilis is a mixed­valence binuclear copper centre. FEBS Lett. 340, 109-113.
  282. Wallace­Williams, S.E., James, C.A., de Vries, S., Saraste, M., Lappalainen, P., van der Oost, J., Fabian, M., Palmer, G. and Woodruff, W.H. (1996) Far­red resonance Raman study of copper A in subunit II of cytochrome c oxidase. J. Am. Chem. Soc. 118, 3986-3987.
  283. Walsh, T.A., Johnson, M.K., Greenwood, C., Barber, D., Springall, J.P. and Thomson, A.J. (1979) Some magnetic properties of Pseudomonas cytochrome oxidase. Biochem. J. 177, 29-39.
  284. Wang, H., Blair, D.F., Ellis, W.R., Gray, H.B. and Chan, S.I. (1986) Temperature dependence of the reduction potential of CuA in carbon monoxide inhibited cytochrome c oxidase. Biochemistry 25, 167-171.
  285. Wang, H., Sauke, T., Debrunner, P.G. and Chan, S.I. (1988) The CO adduct of yeast cytochrome c oxidase. Mössbauer and photolysis studies. J. Biol. Chem. 263, 15260-15263.
  286. Wang, J., Takahashi, S., Hosler, J.P., Mitchell, D.M., Ferguson­Miller, S., Gennis, R.B. and Rousseau, D.L. (1995) Two conformations of the catalytic site in the aa3­type cytochrome c oxidase from Rhodobacter sphaeroides. Biochemistry 34, 9819-9825.
  287. Warne, A., Wang, D.N. and Saraste, M. (1995) Purification and two­dimensional crystallization of bacterial cytochrome oxidases. Eur. J. Biochem. 234, 443-451.
  288. Weber, C., Michel, B. and Bosshard, H.R. (1987) Spectroscopic analysis of the cytochrome c oxidase-cytochrome c complex: circular dichroism and magnetic circular dichroism measurements reveal change of cytochrome c heme geometry imposed by complex formation. Proc. Natl. Acad. Sci. USA 84, 6687-6691.
  289. Weintraub, S.T., Muhoberac, B.B. and Wharton, D.C. (1982) The effects of copper depletion on structural aspects of cytochrome c oxidase. J. Biol. Chem. 257, 4940-4946.
  290. Wever, R., van Gelder, B.F. and DerVartanian, D.V. (1975) Biochemical and biophysical studies on cytochrome c oxidase. XX. Reaction with sulphide. Biochim. Biophys. Acta 387, 189-193.
  291. Wever, R., van Drooge, J.H., Muijsers, A.O., Bakker, E.P. and van Gelder, B.F. (1977) The binding of carbon monoxide to cytochrome c oxidase. Eur. J. Biochem. 73, 149-154.
  292. Williams, K.R., Gamelin, D.R., LaCroix, L.B., Houser, R.P., Tolman, W.B., Mulder, T.C., de Vries, S., Hedman, B., Hodgson, K.O. and Solomon, E.I. (1997) Influence of copper-sulfur covalency and copper-copper bonding on valence delocalization and electron transfer in the CuA site of cytochrome c oxidase. J. Am. Chem. Soc. 119, 613-614.
  293. Wilmanns, M., Lappalainen, P., Kelly, M., Sauer­Eriksson, E. and Saraste, M. (1995) Crystal structure of the membrane­exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center. Proc. Natl. Acad. Sci. USA 92, 11955-11959.
  294. Wilms, J., Lub, J. and Wever, R. (1980) Reactions of mercaptans with cytochrome c oxidase and cytochrome c. Biochim. Biophys. Acta 589, 324-335.
  295. Wittung­Stafshede, P., Malmström, B.G., Sanders, D., Fee, J.A., Winkler, J.R. and Gray, H.B. (1998a) Effect of redox state on the folding free energy of a thermostable electron­transfer metalloprotein: The CuA domain of cytochrome oxidase from Thermus thermophilus. Biochemistry 37, 3172-3177.
  296. Wittung­Stafshede, P., Gomez, E., Ohman, A., Aasa, R., Villahermosa, R.M., Leckner, J., Karlsson, B.G., Sanders, D., Fee, J.A., Winkler, J.R., Malmström, B.G., Gray, H.B. and Hill, M.G. (1999b) High­potential states of blue and purple copper proteins. Biochim. Biophys. Acta 1388, 437-443.
  297. Woodruff, W.H., Dallinger, R.F., Antalis, T.M. and Palmer, G. (1981) Resonance Raman spectroscopy of cytochrome oxidase using Soret excitation: selective enhancement, indicator bands, and structural significance for cytochromes a and a3. Biochemistry 20, 1332-1338.
  298. Woodruff, W.H., Einarsdóttir, Ó, Dyer, R.B., Bagley, K.A., Palmer, G., Atherton, S.J., Goldbeck, R.A., Dawes, T.D. and Kliger, D.S. (1991) Nature and functional implications of the cytochrome a3 transients after photodissociation of CO-cytochrome oxidase. Proc. Natl. Acad. Sci. USA 88, 2588-2592.
  299. Yoshikawa, S. and Caughey, W.S. (1982) Heart cytochrome c oxidase. An infrared study of effects of oxidation state on carbon monoxide binding. J. Biol. Chem. 257, 412-420.
  300. Yoshikawa, S. and Caughey, W.S. (1990) Infrared evidence of cyanide binding to iron and copper sites in bovine heart cytochrome c oxidase. Implications regarding oxygen reduction. J. Biol. Chem. 265, 7945-7958.
  301. Yoshikawa, S. and Caughey, W.S. (1992) Infrared evidence of azide binding to iron, copper, and non­metal sites in heart cytochrome c oxidase. J. Biol. Chem. 267, 9757-9766.
  302. Yoshikawa, S., Choc, M.G., O'Toole, M.C. and Caughey, W.S. (1977) An infrared study of CO binding to heart cytochrome c oxidase and hemoglobin A. Implications re O2 reactions. J. Biol. Chem. 252, 5498-5508.
  303. Yoshikawa, S., Tera, T., Takahashi, Y., Tsukihara, T. and Caughey, W.S. (1988) Crystalline cytochrome c oxidase of bovine heart mitochondrial membrane: composition and x­ray diffraction studies. Proc. Natl. Acad. Sci. USA 85, 1354-1358.
  304. Yoshikawa, S., Mochizuki, M., Zhao, X.­J. and Caughey, W.S. (1995) Effects of overall oxidation state on infrared spectra of heme a3 cyanide in bovine heart cytochrome c oxidase. Evidence of novel mechanistic roles for CuB. J. Biol. Chem. 270, 4270-4279.
  305. Yoshikawa, S., Shinzawa­Itoh, K. and Tsukihara, T. (1998a) Crystal structure of bovine heart cytochrome c oxidase at 2.8 Å resolution. J. Bioenerg. Biomembr. 30, 7-14.
  306. Yoshikawa, S., Shinzawa­Itoh, K., Nakashima, R., Yaono, R., Yamashita, E., Inoue, N., Yao, M., Fei, M.J., Libeu, C.P., Mizushima, T., Yamaguchi, H., Tomizaki, T. and Tsukihara, T. (1998b) Redox­coupled crystal structural changes in bovine heart cytochrome c oxidase. Science 280, 1723-1729.
  307. Young, L.J. (1988) Conformational substates of bovine heart cytochrome c oxidase: the modified Volpe-Caughey variant. Biochemistry 27, 5115-5121.
  308. Young, L.J., Einarsdóttir, Ó., Vossbrink, C.R. and Caughey, W.S. (1984) Infrared spectra of carbon monoxide bound to mitochondria from diverse species and tissues reveal structurally similar cytochrome c oxidase dioxygen reaction sites. Biochem. Biophys. Res. Commun. 123, 247-253.
  309. Yumoto, I., Takahashi, S., Kitagawa, T., Fukumori, Y. and Yamanaka, T. (1993) The molecular features and catalytic activity of CuA­containing aco3­type cytochrome c oxidase from a facultative alkalophilic Bacillus. J. Biochem. (Tokyo) 114, 88-95.
  310. Zamudio, I., Kornblatt, J., Nicholls, P., Li, Y. and Cygler, M. (1990) Preliminary studies on the crystallization of beef heart cytochrome c oxidase by vapor diffusion. Biochem. Biophys. Res. Commun. 169, 1105-1110.
  311. Zaslavsky, D., Sadoski, R.C., Wang, K., Durham, B., Gennis, R.B. and Millett, F. (1998) Single electron reduction of cytochrome c oxidase compound F: Resolution of partial steps by transient spectroscopy. Biochemistry 37, 14910-14916.
  312. Zaslavsky, D., Smirnova, I.A., Ädelroth, P., Brzezinski, P. and Gennis, R.B. (1999) Observation of a novel transient ferryl complex with reduced CuB in cytochrome c oxidase. Biochemistry 38, 2307-2311.
  313. Zhao, X.­J., Sampath, V. and Caughey, W.S. (1994) Infrared characterization of nitric oxide bonding to bovine heart cytochrome c oxidase and myoglobin. Biochem. Biophys. Res. Commun. 204, 537-543.
  314. Zhao, X.­J., Caughey, W.S. and Poyton, R.O. (1995) Fourier transform infrared analysis of carbonyl and nitrosyl complexes of cytochrome­c oxidase from Saccharomyces cerevisiae. Methods Enzymol. 260, 399-406.
  315. Zickermann, V., Verkhovsky, M., Morgan, J., Wikström, M., Anemuller, S., Bill, E., Steffens, G.C. and Ludwig, B. (1995) Perturbation of the CuA site in cytochrome­c oxidase of Paracoccus denitrificans by replacement of Met227 with isoleucine. Eur. J. Biochem. 234, 686-693.
  316. Zickermann, V., Wittershagen, A., Kolbesen, B.O. and Ludwig, B. (1997) Transformation of the CuA redox site in cytochrome c oxidase into a mononuclear copper center. Biochemistry 36, 3232-3236.
  317. Zimmermann, B.H., Nitsche, C.I., Fee, J.A., Rusnak, F. and Münck, E. (1988) Properties of a copper­containing cytochrome ba3: A second terminal oxidase from the extreme thermophile Thermus thermophilus. Proc. Natl. Acad. Sci. USA 85, 5779-5783.
Reviews on cytochrome c oxidase