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Last modified: 9 April 1999

Bibliography on structural studies of fungal, plant and bacterial haem peroxidases

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  1. Adak, S., Bhattacharyya, D.K., Mazumder, A., Bandyopadhyay, U. and Banerjee, R.K. (1995) Concurrent reduction of iodine and oxidation of EDTA at the active site of horseradish peroxidase: Probing the iodine binding site by optical difference spectroscopy and steady state kinetic analysis for the formation of active enzyme-I+-EDTA ternary complex for iodine reductase activity. Biochemistry 34, 12998-13006.
  2. Alam, S.L., Satterlee, J.D., Mauro, J.M., Poulos, T.L. and Erman, J.E. (1995) Proton NMR studies of cytochrome c peroxidase mutant N82A: Hyperfine resonance assignments, identification of two interconverting enzyme ofecies, quantitating the rate of interconversion, and determination of equilibrium constants. Biochemistry 34, 15496-15503.
  3. Alden, R.G. and Ondrias, M.R. (1985) Transient Raman study of horseradish peroxidase. Evidence for a lack of extensive heme pocket relaxation subsequent to carbon monoxide photolysis. J. Biol. Chem. 260, 12194-12197.
  4. Andersson, L.A., Renganathan, V., Chiu, A.A., Loehr, T.M. and Gold, M.H. (1985) Spectral characterization of diarylpropane oxygenase, a novel peroxide­dependent, lignin­degrading heme enzyme. J. Biol. Chem. 260, 6080-6087.
  5. Anni, H., Vanderkooi, J.M., Sharp, K.A., Yonetani, T., Hopkins, S.C., Herenyi, L. and Fidy, J. (1994) Electric field and conformational effects of cytochrome c and solvent on cytochrome c peroxidase studied by high­resolution fluorescence spectroscopy. Biochemistry 33, 3475-3486.
  6. Ator, M.A. and Ortiz de Montellano, P.R. (1987) Protein control of prosthetic heme reactivity. Reaction of substrates with the heme edge of horseradish peroxidase. J. Biol. Chem. 262, 1542-1551.
  7. Ator, M.A., David, S.K. and Ortiz de Montellano, P.R. (1987) Structure and catalytic mechanism of horseradish peroxidase. Regiospecific meso alkylation of the prosthetic heme group by alkylhydrazines. J. Biol. Chem. 262, 14954-14960.
  8. Banci, L., Bertini, I., Pease, E.A., Tien, M. and Turano, P. (1992) 1H NMR investigation of manganese peroxidase from Phanerochaete chrysosporium. A comparison with other peroxidases. Biochemistry 31, 10009-10017.
  9. Banci, L., Bertini, I., Dal Pozzo, L., Del Conte, R. and Tien, M. (1998) Monitoring the role of oxalate in manganese peroxidase. Biochemistry 37, 9009-9015.
  10. Barber, K.R., Rodriguez­Maranon, M.J., Shaw, G.S. and van Huystee, R.B. (1995) Structural influence of calcium on the heme cavity of cationic peanut peroxidase as determined by 1H­NMR spectroscopy. Eur. J. Biochem. 232, 825-833.
  11. Barlow, C.H., Ohlsson, P.I. and Paul, K.G. (1976) Infrared spectroscopic studies of carbonyl horseradish peroxidases. Biochemistry 15, 2225-2229.
  12. Bedard, P. and Mabrouk, P.A. (1997) Resonance Raman spectroscopy of soybean peroxidase. Biochem. Biophys. Res. Commun. 240, 65-67.
  13. Behere, D.V., Gonzalez­Vergara, E. and Goff, H.M. (1985a) Comparison of heme environments and proximal ligands in peroxidases and other hemoproteins through carbon­13 nuclear magnetic resonance spectroscopy of carbon monoxide complexes. Biochem. Biophys. Res. Commun. 131, 607-613.
  14. Behere, D.V., Gonzalez­Vergara, E. and Goff, H.M. (1985b) Unique cyanide nitrogen­15 nuclear magnetic resonance chemical shift values for cyano­peroxidase complexes. Relevance to the heme active­site structure and mechanism of peroxide activation. Biochim. Biophys. Acta 832, 319-325.
  15. Benko, B. and Yu, N.T. (1983) Resonance Raman studies of nitric oxide binding to ferric and ferrous hemoproteins: Detection of Fe(III)-NO stretching, Fe(III)-N-O bending, and Fe(II)-N-O bending vibrations. Proc. Natl. Acad. Sci. USA 80, 7042-7046.
  16. Berglund, J., Pascher, T., Winkler, J.R. and Gray, H.B. (1997) Photoinduced oxidation of horseradish peroxidase. J. Am. Chem. Soc. 119, 2464-2469.
  17. Bonagura, C.A., Sundaramoorthy, M., Pappa, H.S., Patterson, W.R. and Poulos, T.L. (1996) An engineered cation site in cytochrome c peroxidase alters the reactivity of the redox active tryptophan. Biochemistry 35, 6107-6115.
  18. Boswell, A.P., McClune, G.J., Moore, G.R., Williams, R.J.P., Pettigrew, G.W., Inubishi, T., Yonetani, T. and Harris, D.E. (1980) Nuclear­magnetic­resonance study of the interaction of cytochrome c with cytochrome c peroxidase. Biochem. Soc. Trans. 8, 637-638.
  19. Braithwaite, A. (1976) Unit cell dimensions of crystalline horseradish peroxidase. J. Mol. Biol. 106, 229-230.
  20. Browett, W.R. and Stillman, M.J. (1981) Evidence for heme pi cation radical species in compound I of horseradish peroxidase and catalase. Biochim. Biophys. Acta 660, 1-7.
  21. Browett, W.R., Gasyna, Z. and Stillman, M.J. (1983) The temperature dependence of the MCD spectrum of horseradish peroxidase compound I. Biochem. Biophys. Res. Commun. 112, 515-520.
  22. Bujons, J., Dikiy, A., Ferrer, J.C., Banci, L. and Mauk, A.G. (1997) Charge reversal of a critical active­site residue of cytochrome­c peroxidase. Characterization of the Arg48->Glu variant. Eur. J. Biochem. 243, 72-84.
  23. Casella, L., Gullotti, M., Ghezzi, R., Poli, S., Beringhelli, T., Colonna, S. and Carrea, G. (1992) Mechanism of enantioselective oxygenation of sulfides catalyzed by chloroperoxidase and horseradish peroxidase. Spectral studies and characterization of enzyme-substrate complexes. Biochemistry 31, 9451-9459.
  24. Champion, P.M., Chiang, R., Münck, E., Debrunner, P.G. and Hager, L.P. (1975) Mössbauer investigations of high­spin ferrous heme proteins. II. Chloroperoxidase, horseradish peroxidase, and hemoglobin. Biochemistry 14, 4159-4166.
  25. Chance, B., Powers, L., Ching, Y., Poulos, T.L., Schonbaum, G.R., Yamazaki, I. and Paul, K.G. (1984) X­ray absorption studies of intermediates in peroxidase activity. Arch. Biochem. Biophys. 235, 596-611.
  26. Chance, M., Powers, L., Poulos, T. and Chance, B. (1986) Cytochrome c peroxidase compound ES is identical with horseradish peroxide compound I in iron-ligand distances. Biochemistry 25, 1266-1270.
  27. Chang, C.S., Yamazaki, I., Sinclair, R., Khalid, S. and Powers, L. (1993) pH dependence of the active site of horseradish peroxidase compound II. Biochemistry 32, 923-928.
  28. Cheek, J., Mandelman, D., Poulos, T.L. and Dawson, J.H. (1999) A study of the K+­site mutant of ascorbate peroxidase: mutations of protein residues on the proximal side of the heme cause changes in iron ligation on the distal side. J. Biol. Inorg. Chem. 4, 64-72.
  29. Choinowski, T., Blodig, W., Winterhalter, K.H. and Piontek, K. (1999) The crystal structure of lignin peroxidase at 1.70 Å resolution reveals a hydroxy group on the Cß of tryptophan 171: A novel radical site formed during the redox cycle. J. Mol. Biol. 286, 809-827.
  30. Choudhury, K., Sundaramoorthy, M., Mauro, J.M. and Poulos, T.L. (1992) Conversion of the proximal histidine ligand to glutamine restores activity to an inactive mutant of cytochrome c peroxidase. J. Biol. Chem. 267, 25656-25659.
  31. Choudhury, K., Sundaramoorthy, M., Hickman, A., Yonetani, T., Woehl, E., Dunn, M.F. and Poulos, T.L. (1994) Role of the proximal ligand in peroxidase catalysis. Crystallographic, kinetic, and spectral studies of cytochrome c peroxidase proximal ligand mutants. J. Biol. Chem. 269, 20239-20249.
  32. Chuang, W.J. and van Wart, H.E. (1992) Resonance Raman spectra of horseradish peroxidase and bovine liver catalase compound I species. Evidence for predominant 2A2u pi­cation radical ground state configurations. J. Biol. Chem. 267, 13293-13301.
  33. Das, T.K. and Mazumdar, S. (1995) pH­induced conformational perturbation in horseradish peroxidase. Picosecond tryptophan fluorescence studies on native and cyanide­modified enzymes. Eur. J. Biochem. 227, 823-828.
  34. Dasgupta, S., Rousseau, D.L., Anni, H. and Yonetani, T. (1989) Structural characterization of cytochrome c peroxidase by resonance Raman scattering. J. Biol. Chem. 264, 654-662.
  35. de Ropp, J.S., La Mar, G.N., Wariishi, H. and Gold, M.H. (1991) NMR study of the active site of resting state and cyanide­inhibited lignin peroxidase from Phanerochaete chrysosporium. Comparison with horseradish peroxidase. J. Biol. Chem. 266, 15001-15008.
  36. de Ropp, J.S., Chen, Z. and La Mar, G.N. (1995) Identification of residues in the aromatic substrate binding site of horseradish peroxidase by 1H NMR studies on isozymes. Biochemistry 34, 13477-13484.
  37. de Ropp, J.S., Mandal, P.K., Brauer, S.L. and La Mar, G.N. (1997) Solution NMR study of the electronic and molecular structure of the heme cavity in high­spin, resting state horseradish peroxidase. J. Am. Chem. Soc. 119, 4732-4739.
  38. de Ropp, J.S., Mandal, P.K. and La Mar, G.N. (1999) Solution 1H NMR investigation of the heme cavity and substrate binding site in cyanide­inhibited horseradish peroxidase. Biochemistry 38, 1077-1086.
  39. Doyle, W.A., Blodig, W., Veitch, N.C., Piontek, K. and Smith, A.T. (1998) Two substrate interaction sites in lignin peroxidase revealed by site­directed mutagenesis. Biochemistry 37, 15097-15105.
  40. Edwards, S.L. and Poulos, T.L. (1990) Ligand binding and structural perturbations in cytochrome c peroxidase. A crystallographic study. J. Biol. Chem. 265, 2588-2595.
  41. Edwards, S.L., Poulos, T.L. and Kraut, J. (1984) The crystal structure of fluoride­inhibited cytochrome c peroxidase. J. Biol. Chem. 259, 12984-12988.
  42. Edwards, S.L., Nguyen, H.X., Hamlin, R.C. and Kraut, J. (1987) Crystal structure of cytochrome c peroxidase compound I. Biochemistry 26, 1503-1511.
  43. Edwards, S.L., Kraut, J. and Poulos, T.L. (1988a) Crystal structure of nitric oxide inhibited cytochrome c peroxidase. Biochemistry 27, 8074-8081.
  44. Edwards, S.L., Mauro, J.M., Fishel, L.A., Wang, J.M., Miller, M.A., Xuong, N.­H. and Kraut, J. (1988b) Where is the radical in compound I of cytochrome c peroxidase? Clues from crystallography and mutagenesis. Prog. Clin. Biol. Res. 274, 463-475.
  45. Edwards, S.L., Raag, R., Wariishi, H., Gold, M.H. and Poulos, T.L. (1993) Crystal structure of lignin peroxidase. Proc. Natl. Acad. Sci. USA 90, 750-754.
  46. Erman, J.E., Vitello, L.B., Miller, M.A., Shaw, A., Brown, K.A. and Kraut, J. (1993) Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I. Biochemistry 32, 9798-9806.
  47. Evangelista­Kirkup, R., Crisanti, M., Poulos, T.L. and Spiro, T.G. (1985) Resonance Raman spectroscopy shows different temperature­dependent coordination equilibria for native horseradish and cytochrome c peroxidase. FEBS Lett. 190, 221-226.
  48. Evangelista­Kirkup, R., Smulevich, G. and Spiro, T.G. (1986) Alternative carbon monoxide binding modes for horseradish peroxidase studied by resonance Raman spectroscopy. Biochemistry 25, 4420-4425.
  49. Feis, A., Marzocchi, M.P., Paoli, M. and Smulevich, G. (1994) Spin state and axial ligand bonding in the hydroxide complexes of metmyoglobin, methemoglobin, and horseradish peroxidase at room and low temperatures. Biochemistry 33, 4577-4583.
  50. Feis, A., Rodriguez­Lopez, J.N., Thorneley, R.N.F. and Smulevich, G. (1998) The distal cavity structure of carbonyl horseradish peroxidase as probed by the resonance Raman spectra of His42Leu and Arg38Leu mutants. Biochemistry 37, 13575-13581.
  51. Felton, R.H., Romans, A.Y., Yu, N.T. and Schonbaum, G.R. (1976) Laser Raman spectra of oxidized hydroperoxidases. Biochim. Biophys. Acta 434, 82-89.
  52. Fernández, C.O., Podestá, O., Converso, D.A., Fernández, M.E. and Vila, A.J. (1997) A biophysical characterization of the iron coordination environment in wheat germ peroxidase. J. Biol. Inorg. Chem. 2, 218-224.
  53. Fernandez, M., Frydman, R.B., Hurst, J. and Buldain, G. (1993) Structure/activity relationships in porphobilinogen oxygenase and horseradish peroxidase. An analysis using synthetic hemins. Eur. J. Biochem. 218, 251-259.
  54. Ferrer, J.C., Turano, P., Banci, L., Bertini, I., Morris, I.K., Smith, K.M. Smith, M. and Mauk, A.G. (1994) Active site coordination chemistry of the cytochrome c peroxidase Asp235Ala variant: spectroscopic and functional characterization. Biochemistry 33, 7819-7829.
  55. Ferri, T., Poscia, A. and Santucci, R. (1998) Direct electrochemistry of membrane­entrapped horseradish peroxidase. Part I. A voltammetric and spectroscopic study. Bioelectrochem. Bioenergetics 44, 177-181.
  56. Finzel, B.C., Poulos, T.L. and Kraut, J. (1984) Crystal structure of yeast cytochrome c peroxidase refined at 1.7­Å resolution. J. Biol. Chem. 259, 13027-13036.
  57. Fishel, L.A., Villafranca, J.E., Mauro, J.M. and Kraut, J. (1987) Yeast cytochrome c peroxidase: mutagenesis and expression in Escherichia coli show tryptophan­51 is not the radical site in compound I. Biochemistry 26, 351-360.
  58. Fishel, L.A., Farnum, M.F., Mauro, J.M., Miller, M.A., Kraut, J., Liu, Y.J., Tan, X.L. and Scholes, C.P. (1991) Compound I radical in site­directed mutants of cytochrome c peroxidase as probed by electron paramagnetic resonance and electron­nuclear double resonance. Biochemistry 30, 1986-1996.
  59. Fitzgerald, M.M., Churchill, M.J., McRee, D.E. and Goodin, D.B. (1994) Small molecule binding to an artificially created cavity at the active site of cytochrome c peroxidase. Biochemistry 33, 3807-3818.
  60. Fitzgerald, M.M., Trester, M.L., Jensen, G.M., McRee, D.E. and Goodin, D.B. (1995) The role of aspartate­235 in the binding of cations to an artificial cavity at the radical site of cytochrome c peroxidase. Protein Science 4, 1844-1850.
  61. Fitzgerald, M.M., Musah, R.A., McRee, D.E. and Goodin, D.B. (1996) A ligand­gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity. Nature Struct. Biol. 3, 626-631.
  62. Fox, T., Ferreira­Rajabi, L., Hill, B.C. and English, A.M. (1993) Quenching of intrinsic fluorescence of yeast cytochrome c peroxidase by covalently­ and noncovalently­bound quenchers. Biochemistry 32, 6938-6943.
  63. Fraaije, M.W., Roubroeks, H.P., Hagen, W.R. and van Berkel, W.J. (1996) Purification and characterization of an intracellular catalase­peroxidase from Penicillium simplicissimum. Eur. J. Biochem. 235, 192-198.
  64. Fukuyama, K., Kunishima, N., Amada, F., Kubota, T. and Matsubara, H. (1995) Crystal structures of cyanide­ and triiodide­bound forms of Arthromyces ramosus peroxidase at different pH values. Perturbations of active site residues and their implication in enzyme catalysis. J. Biol. Chem. 270, 21884-21892.
  65. Fukuyama, K., Sato, K., Itakura, H., Takahashi, S. and Hosoya, T. (1997) Binding of iodide to Arthromyces ramosus peroxidase investigated with X­ray crystallographic analysis, 1H and 127I NMR spectroscopy, and steady­state kinetics. J. Biol. Chem. 272, 5752-5756.
  66. Fülöp, V., Phizackerley, R.P., Soltis, S.M., Clifton, I.J., Wakatsuki, S., Erman, J., Hajdu, J. and Edwards, S.L. (1994) Laue diffraction study on the structure of cytochrome c peroxidase compound I. Structure 2, 201-208.
  67. Gajhede, M., Schuller, D.J., Henriksen, A., Smith, A.T. and Poulos, T.L. (1997) Crystal structure of horseradish peroxidase C at 2.15 Å resolution. Nature Struct. Biol. 4, 1032-1038.
  68. Gasyna, Z., Browett, W.R. and Stillman, M.J. (1988) Low­temperature magnetic circular dichroism studies of the photoreaction of horseradish peroxidase compound I. Biochemistry 27, 2503-2509.
  69. Glumoff, T., Winterhalter, K.H. and Smit, J.D.G. (1989) Monoclinic crystals of lignin peroxidase. FEBS Lett. 257, 59-62.
  70. Goodin, D.B. and McRee, D.E. (1993) The Asp­His­Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme. Biochemistry 32, 3313-3324.
  71. Goodin, D.B., Mauk, A.G. and Smith, M. (1986) Studies of the radical species in compound ES of cytochrome c peroxidase altered by site­directed mutagenesis. Proc. Natl. Acad. Sci. USA 83, 1295-1299.
  72. Goodin, D.B., Mauk, A.G. and Smith, M. (1987) The peroxide complex of yeast cytochrome c peroxidase contains two distinct radical species, neither of which resides at methionine 172 or tryptophan 51. J. Biol. Chem. 262, 7719-7724.
  73. Goodin, D.B., Davidson, M.G., Roe, J.A., Mauk, A.G. and Smith, M. (1991) Amino acid substitutions at tryptophan­51 of cytochrome c peroxidase: Effects on coordination, species preference for cytochrome c, and electron transfer. Biochemistry 30, 4953-4962.
  74. Han, Y.­H., Shin, K.­S., Youn, H.­D., Hah, Y.C. and Kang, S.­O. (1996) Mode of action and active site of an extracellular peroxidase from Pleurotus ostreatus. Biochem. J. 314, 421-426.
  75. Haque, M.E., Debnath, D., Basak, S. and Chakrabarti, A. (1999) Structural changes of horseradish peroxidase in presence of low concentrations of urea. Eur. J. Biochem. 259, 269-274. Spectroscopy
  76. Hashimoto, S. and Takeuchi, H. (1998) Detection of UV resonance Raman bands of the distal histidine in cyanide­bound horseradish peroxidase: Evidence for two hydrogen bonding states of the imidazolium side chain. J. Am. Chem. Soc. 120, 11012-11013.
  77. Hashimoto, S., Teraoka, J., Inubushi, T., Yonetani, T. and Kitagawa, T. (1986) Resonance Raman study on cytochrome c peroxidase and its intermediate. Presence of the Fe(IV)=O bond in compound ES and heme­linked ionization. J. Biol. Chem. 261, 11110-11118.
  78. Henriksen, A., Petersen, J.F.W., Svensson, A., Hejgaard, J., Welinder, K.G. and Gajhede, M. (1992) Crystallization and preliminary X­ray diffraction studies of a peroxidase from barley grain. J. Mol. Biol. 228, 690-692.
  79. Henriksen, A., Gajhede, M., Baker, P., Smith, A.T. and Burke, J.F. (1995) Crystallization and preliminary X­ray studies of recombinant horseradish peroxidase. Acta Crystallogr. D51, 121-123.
  80. Henriksen, A., Schuller, D.J., Meno, K., Welinder, K.G., Smith, A.T. and Gajhede, M. (1998) Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X­ray crystallography. Biochemistry 37, 8054-8060.
  81. Hildebrandt, P., English, A.M. and Smulevich, G. (1992) Cytochrome c and cytochrome c peroxidase complex as studied by resonance Raman spectroscopy. Biochemistry 31, 2384-2392.
  82. Hill, A.P., Modi, S., Sutcliffe, M.J., Turner, D.D., Gilfoyle, D.J., Smith, A.T., Tam, B.M. and Lloyd, E. (1997) Chemical, spectroscopic and structural investigation of the substrate­binding site in ascorbate peroxidase. Eur. J. Biochem. 248, 347-354.
  83. Holzbaur, I.E., English, A.M. and Ismail, A.A. (1996a) FTIR study of the thermal denaturation of horseradish and cytochrome c peroxidases in D2O. Biochemistry 35, 5488-5494.
  84. Holzbaur, I.E., English, A.M. and Ismail, A.A. (1996b) Infrared spectra of carbonyl horseradish peroxidase and its substrate complexes: Characterization of pH­dependent conformers. J. Am. Chem. Soc. 118, 3354-3359.
  85. Hori, H. and Yonetani, T. (1985) Powder and single­crystal electron paramagnetic resonance studies of yeast cytochrome c peroxidase and its peroxide and its peroxide compound, Compound ES. J. Biol. Chem. 260, 349-355.
  86. Hori, H., Tsubaki, M., Yu, N.T. and Yonetani, Y. (1991) Light absorption, electron paramagnetic resonance and resonance Raman characteristics of nitridochromium(V) protoporphyrin­IX and its reconstituted hemoproteins. Biochim. Biophys. Acta 1077, 392-399.
  87. Houseman, A.L., Doan, P.E., Goodin, D.B. and Hoffman, B.M. (1993) Comprehensive explanation of the anomalous EPR spectra of wild­type and mutant cytochrome c peroxidase compound ES. Biochemistry 32, 4430-4443.
  88. Howes, B.D., Rodriguez­Lopez, J.N., Smith, A.T. and Smulevich, G. (1997) Mutation of distal residues of horseradish peroxidase: Influence on substrate binding and cavity properties. Biochemistry 36, 1532-1543.
  89. Itakura, H., Oda, Y. and Fukuyama, K. (1997) Binding mode of benzhydroxamic acid to Arthromyces ramosus peroxidase shown by X­ray crystallographic analysis of the complex at 1.6 Å resolution. FEBS Lett. 412, 107-110.
  90. Jeng, M.­F., Englander, S.W., Pardue, K., Rogalskyj, J.S. and McLendon, G. (1994) Structural dynamics in an electron­transfer complex. Nature Struct. Biol. 1, 234-238.
  91. Johjima, T., Wariishi, H. and Tanaka, H. (1996) The effect of ligand field strength on nonresonance Raman characteristics of hemoproteins. Biochem. Biophys. Res. Commun. 226, 601-606.
  92. Johnsson, K., Froland, W.A. and Schultz, P.G. (1997) Overexpression, purification, and characterization of the catalase­peroxidase KatG from Mycobacterium tuberculosis. J. Biol. Chem. 272, 2834-2840.
  93. Khindaria, A. and Aust, S.D. (1996) EPR detection and characterization of lignin peroxidase porphyrin pi­cation radical. Biochemistry 35, 13107-13111.
  94. Khindaria, A., Grover, T.A. and Aust, S.D. (1995a) Evidence for formation of the veratryl alcohol cation radical by lignin peroxidase. Biochemistry 34, 6020-6025.
  95. Khindaria, A., Barr, D.P. and Aust, S.D. (1995b) Lignin peroxidases can also oxidize manganese. Biochemistry 34, 7773-7779.
  96. Khindaria, A., Yamazaki, I. and Aust, S.D. (1995c) Veratryl alcohol oxidation by lignin peroxidase. Biochemistry 34, 16860-16869.
  97. Khindaria, A., Yamazaki, I. and Aust, S.D. (1996) Stabilization of the veratryl alcohol cation radical by lignin peroxidase. Biochemistry 35, 6418-6424.
  98. Kincaid, J.R., Zheng, Y., Al­Mustafa, J. and Czarnecki, K. (1996) Resonance Raman spectra of native and mesoheme­reconstituted horseradish peroxidase and their catalytic intermediates. J. Biol. Chem. 271, 28805-28811.
  99. Kishi, K., Kusters­van Someren, M., Mayfield, M.B., Sun, J., Loehr, T.M. and Gold, M.H. (1996) Characterization of manganese(II) binding site mutants of manganese peroxidase. Biochemistry 35, 8986-8994.
  100. Kishi, K., Hildebrand, D.P., Kusters­van Someren, M., Gettemy, J., Mauk, A.G. and Gold, M.H. (1997) Site­directed mutations at phenylalanine­190 of manganese peroxidase: Effects on stability, function, and coordination. Biochemistry 36, 4268-4277.
  101. Kobayashi, K., Tamura, M., Hayashi, K., Hori, H. and Morimoto, H. (1980) Electron paramagnetic resonance and optical absorption spectrum of the pentacoordinated ferrihemoproteins. J. Biol. Chem. 255, 2239-2242.
  102. Kornblatt, J.A., English, A.M. and Hui Bon Hoa, G. (1986) The effects of pressure on yeast cytochrome c peroxidase. Eur. J. Biochem. 159, 39-43.
  103. Kumar, C., Naqui, A., Powers, L., Ching, Y.C. and Chance, B. (1988) Does the peroxide compound of cytochrome oxidase contain a ferryl iron? J. Biol. Chem. 263, 7159-7163.
  104. Kunishima, N., Fukuyama, K., Matsubara, H., Hatanaka, H., Shibano, Y. and Amachi, T. (1994) Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1.9 Å resolution. Structural comparisons with the lignin and cytochrome c peroxidases. J. Mol. Biol. 235, 331-344.
  105. Kunishima, N., Amada, F., Fukuyama, K., Kawamoto, M., Matsunaga, T. and Matsubara, H. (1996) Pentacoordination of the heme iron of Arthromyces ramosus peroxidase shown by a 1.8 Å resolution crystallographic study at pH 4.5. FEBS Lett. 378, 291-294.
  106. Lasagna, M., Gratton, E., Jameson, D.M. and Brunet, J.E. (1999) Apohorseradish peroxidase unfolding and refolding: Intrinsic tryptophan fluorescence studies. Biophys. J. 76, 443-450.
  107. Lee, H.C., Cummings, K., Hall, K., Hager, L.P. and Oldfield, E. (1988) Oxygen­17 nuclear magnetic resonance spectroscopic studies of carbonmonoxyperoxidases. J. Biol. Chem. 263, 16118-16124.
  108. Liu, K., Williams, J., Lee, H., Fitzgerald, M.M., Jensen, G.M., Goodin, D.B. and McDermott, A.E. (1998) Solid­state deuterium NMR of imidazole ligands in cytochrome c peroxidase. J. Am. Chem. Soc. 120, 10199-10202.
  109. López­Garriga, J.J., Oertling, W.A., Kean, R.T., Hoogland, H., Wever, R. and Babcock, G.T. (1990) Metal-ligand vibrations of cyanoferric myeloperoxidase and cyanoferric horseradish peroxidase: evidence for a constrained heme pocket in myeloperoxidase. Biochemistry 29, 9387-9395.
  110. Mabrouk, P.A. and Spiro, T.G. (1998) New insights into horseradish peroxidase function in benzene from resonance Raman spectroscopy. J. Am. Chem. Soc. 120, 10303-10309.
  111. McRee, D.E., Jensen, G.M., Fitzgerald, M.M., Siegel, H.A. and Goodin, D.B. (1994) Construction of a bisaquo heme enzyme and binding by exogenous ligands. Proc. Natl. Acad. Sci. USA 91, 12847-12851.
  112. Makino, R., Uno, T., Nishimura, Y., Iizuka, T., Tsuboi, M. and Ishimura, Y. (1986) Coordination structures and reactivities of compound II in iron and manganese horseradish peroxidases. A resonance Raman study. J. Biol. Chem. 261, 8376-8382.
  113. Magonov, S.N., Davydov, R.M., Blumenfeld, L.A., Arutiunian, A.M. and Sharonov, Yu.A. (1978) Absorption and magnetic circular dichroism spectra of heme proteins in nonequilibrium states. III. Complexes of peroxidase. Mol. Biol. (Moscow) 12, 1191-1197.
  114. Mandelman, D., Schwarz, F.P., Li, H. and Poulos, T.L. (1998a) The role of quaternary interactions on the stability and activity of ascorbate peroxidase. Protein Science 7, 2089-2098.
  115. Mandelman, D., Jamal, J. and Poulos, T.L. (1998b) Identification of two electron­transfer sites in ascorbate peroxidase using chemical modification, enzyme kinetics, and crystallography. Biochemistry 37, 17610-17617.
  116. Marcinkeviciene, J.A., Magliozzo, R.S. and Blanchard, J.S. (1995) Purification and characterization of the Mycobacterium smegmatis catalase­peroxidase involved in isoniazid activation. J. Biol. Chem. 270, 22290-22295.
  117. Mauk, M.R., Kishi, K., Gold, M.H. and Mauk, A.G. (1998) pH­linked binding of Mn(II) to manganese peroxidase. Biochemistry 37, 6767-6771.
  118. Menyhárd, D.K. and Náray­Szabó, G. (1999) Electrostatic effect on electron transfer at the active site of heme peroxidases: A comparative molecular orbital study on cytochrome c peroxidase and ascorbate peroxidase. J. Phys. Chem. B103, 227-233. Computation
  119. Miller, M.A., Han, G.W. and Kraut, J. (1994a) A cation binding motif stabilizes the compound I radical of cytochrome c peroxidase. Proc. Natl. Acad. Sci. USA 91, 11118-11122.
  120. Miller, M.A., Shaw, A. and Kraut, J. (1994b) 2.2 Å structure of oxy­peroxidase as a model for the transient enzyme:peroxide complex. Nature Struct. Biol. 1, 524-531.
  121. Miller, V.P., Goodin, D.B., Friedman, A.E., Hartmann, C. and Ortiz de Montellano, P.R. (1995) Horseradish peroxidase Phe172->Tyr mutant. Sequential formation of compound I with a porphyrin radical cation and a protein radical. J. Biol. Chem. 270, 18413-18419.
  122. Mino, Y., Wariishi, H., Blackburn, N.J., Loehr, T.M. and Gold, M.H. (1988) Spectral characterization of manganese peroxidase, an extracellular heme enzyme from the lignin­degrading basidiomycete, Phanerochaete chrysosporium. J. Biol. Chem. 263, 7029-7036.
  123. Moench, S.J., Chroni, S., Lou, B.S., Erman, J.E. and Satterlee, J.D. (1992) Proton NMR comparison of noncovalent and covalently cross­linked complexes of cytochrome c peroxidase with horse, tuna, and yeast ferricytochromes c. Biochemistry 31, 3661-3670.
  124. Mondal, M.S., Goodin, D.B. and Armstrong, F.A. (1998) Simultaneous voltammetric comparisons of reduction potentials, reactivities, and stabilities of the high­potential catalytic states of wild­type and distal­pocket mutant (W51F) yeast cytochrome c peroxidase. J. Am. Chem. Soc. 120, 6270-6276 [published erratum J. Am. Chem. Soc. 120, 13284 (1998)].
  125. Morimoto, A., Tanaka, M., Takahashi, S., Ishimori, K., Hori, H. and Morishima, I. (1998) Detection of a tryptophan radical as an intermediate species in the reaction of horseradish peroxidase mutant (Phe­221->Trp) and hydrogen peroxide. J. Biol. Chem. 273, 14753-14760.
  126. Morishima, I., Ogawa, S., Inubushi, T., Yonezawa, T. and Iizuka, T. (1977) Nuclear magnetic resonance studies of hemoproteins. Acid­alkaline transition, ligand binding characteristics, and structure of the heme environments in horseradish peroxidase. Biochemistry 16, 5109-5115.
  127. Morishima, I., Ogawa, S. and Yamada, H. (1980) High­pressure proton nuclear magnetic resonance studies of hemoproteins. Pressure­induced structural change in heme environments of myoglobin, hemoglobin, and horseradish peroxidase. Biochemistry 19, 1569-1575.
  128. Morishima, I., Kurono, M. and Shiro, Y. (1986) Presence of endogenous calcium ion in horseradish peroxidase. Elucidation of metal­binding site by substitutions of divalent and lanthanide ions for calcium and use of metal­induced NMR (1H and 113Cd) resonances. J. Biol. Chem. 261, 9391-9399.
  129. Mukai, M., Nagano, S., Tanaka, M., Ishimori, K., Morishima, I., Ogura, T., Watanabe, Y. and Kitagawa, T. (1997) Effects of concerted hydrogen bonding of distal histidine on active site structures of horseradish peroxidase. Resonance Raman studies with Asn70 mutants. J. Am. Chem. Soc. 119, 1758-1766.
  130. Musah, R.A. and Goodin, D.B. (1997) Introduction of novel substrate oxidation into cytochrome c peroxidase by cavity complementation: Oxidation of 2­aminothiazole and covalent modification of the enzyme. Biochemistry 36, 11665-11674.
  131. Myers, D. and Palmer, G. (1985) Magnetic circular dichroism studies on the heme and tryptophan components of cytochrome c peroxidase. J. Biol. Chem. 260, 3887-3890.
  132. Mylrajan, M., Valli, K., Wariishi, H., Gold, M.H. and Loehr, T.M. (1990) Resonance Raman spectroscopic characterization of compound III of lignin peroxidase. Biochemistry 29, 9617-9623.
  133. Nagano, S., Tanaka, M., Ishimori, K., Watanabe, Y. and Morishima, I. (1996) Catalytic roles of the distal site asparagine­histidine couple in peroxidases. Biochemistry 35, 14251-14258.
  134. Nakamura, M. and Hayashi, T. (1992) Oxidation mechanism of vitamin E analogue (Trolox C, 6­hydroxy­2,2,5,7,8­pentamethylchroman) and vitamin E by horseradish peroxidase and myoglobin. Arch. Biochem. Biophys. 299, 313-319.
  135. Neri, F., Kok, D., Miller, M.A. and Smulevich, G. (1997) Fluoride binding in hemoproteins: The importance of the distal cavity structure. Biochemistry 36, 8947-8953 [published erratum Biochemistry 37, 8268 (1998)].
  136. Neri, F., Indiani, C., Welinder, K.G. and Smulevich, G. (1998) Mutation of the distal arginine in Coprinus cinereus peroxidase: Structural implications. Eur. J. Biochem. 251, 830-838.
  137. Newmyer, S.L., Sun, J., Loehr, T.M. and Ortiz de Montellano, P.R. (1996) Rescue of the horseradish peroxidase His­170->Ala mutant activity by imidazole: Importance of proximal ligand tethering. Biochemistry 35, 12788-12795.
  138. Nie, G. and Aust, S.D. (1997) Spectral changes of lignin peroxidase during reversible inactivation. Biochemistry 36, 5113-5119.
  139. Nissum, M., Neri, F., Mandelman, D., Poulos, T.L. and Smulevich, G. (1998) Spectroscopic characterization of recombinant pea cytosolic ascorbate peroxidase: Similarities and differences with cytochrome c peroxidase. Biochemistry 37, 8080-8087.
  140. Nozawa, T., Kobayashi, N. and Hatano, M. (1976) Magnetic circular dichroism studies on horseradish peroxidase. Biochim. Biophys. Acta 427, 652-662.
  141. Nozawa, T., Kobayashi, N., Hatano, M., Ueda, M. and Sogami, M. (1980) Magnetic circular dichroism on oxygen complexes of hemoproteins: correlation between magnetic circular dichroism magnitude and electronic structures of oxygen complexes. Biochim. Biophys. Acta 626, 282-290.
  142. Oertling, W.A. and Babcock, G.T. (1988) Time­resolved and static resonance Raman spectroscopy of horseradish peroxidase intermediates. Biochemistry 27, 3331-3338.
  143. Palaniappan, V. and Terner, J. (1989) Resonance Raman spectroscopy of horseradish peroxidase derivatives and intermediates with excitation in the near ultraviolet. J. Biol. Chem. 264, 16046-16053.
  144. Park, K.D., Guo, K.M., Adebodun, F., Chiu, M.L., Sligar, S.G. and Oldfield, E. (1991) Distal and proximal ligand interactions in heme proteins: correlations between C-O and Fe-C vibrational frequencies, oxygen­17 and carbon­13 nuclear magnetic resonance chemical shifts, and oxygen­17 nuclear quadrupole coupling constants in C17O­ and 13CO­labeled species. Biochemistry 30, 2333-2347.
  145. Patterson, W.R. and Poulos, T.L. (1994) Characterization and crystallization of recombinant pea cytosolic ascorbate peroxidase. J. Biol. Chem. 269, 17020-17024.
  146. Patterson, W.R. and Poulos, T.L. (1995) Crystal structure of recombinant pea cytosolic ascorbate peroxidase. Biochemistry 34, 4331-4341.
  147. Patterson, W.R., Poulos, T.L. and Goodin, D.B. (1995) Identification of a porphyrin pi cation radical in ascorbate peroxidase compound I. Biochemistry 34, 4342-4335.
  148. Pelletier, H. and Kraut, J. (1992) Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c. Science 258, 1748-1755.
  149. Penner­Hahn, J.E., McMurry, T.J., Renner, M., Latos­Grazynsky, L., Eble, K.S., Davis, I.M., Balch, A.L., Groves, J.T., Dawson, J.H. and Hodgson, K.O. (1983) X­ray absorption spectroscopic studies of high valent iron porphyrins. Horseradish peroxidase compounds I and II and synthetic models. J. Biol. Chem. 258, 12761-12764.
  150. Perie, F.H., Sheng, D. and Gold, M.H. (1996) Purification and characterization of two manganese peroxidase isozymes from the white­rot basidiomycete Dichomitus squalens. Biochim. Biophys. Acta 1297, 139-148.
  151. Petersen, J.F.W., Tams, J.W., Vind, J., Svensson, A., Dalbøge, H., Welinder, K.G. and Larsen, S. (1993) Crystallization and X­ray diffraction analysis of recombinant Coprinus cinereus peroxidase. J. Mol. Biol. 232, 989-991.
  152. Petersen, J.F.W., Kadziola, A. and Larsen, S. (1994) Three­dimensional structure of a recombinant peroxidase from Coprinus cinereus at 2.6 Å resolution. FEBS Lett. 339, 291-296.
  153. 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.
  154. Pettigrew, G.W., Prazeres, S., Costa, C., Palma, P.N., Krippahl, L., Moura, I. and Moura, J.J.G. (1999) The structure of an electron transfer complex containing a cytochrome c and a peroxidase. J. Biol. Chem. 274, 11383-11389.
  155. Pierattelli, R., Banci, L. and Turner, D.L. (1996) Indirect determination of magnetic susceptibility tensors in peroxidases: A novel approach to structure elucidation by NMR. J. Biol. Inorg. Chem. 1, 320-329.
  156. Piontek, K., Glumoff, T. and Winterhalter, K. (1993) Low pH crystal structure of glycosylated lignin peroxidase from Phanerochaete chrysosporium at 2.5 Å resolution. FEBS Lett. 315, 119-124.
  157. Poulos, T.L., Freer, S.T., Alden, R.A., Xuong, N.­H., Edwards, S.L., Hamlin, R.C. and Kraut, J. (1978) Crystallographic determination of the heme orientation and location of the cyanide binding site in yeast cytochrome c peroxidase. J. Biol. Chem. 253, 3730-3735.
  158. Poulos, T.L., Freer, S.T., Alden, R.A., Edwards, S.L., Skogland, U., Takio, K., Eriksson, B., Xuong, N.­H., Yonetani, T. and Kraut, J. (1980) The crystal structure of cytochrome c peroxidase. J. Biol. Chem. 255, 575-580.
  159. Poulos, T.L., Sheriff, S. and Howard, A.J. (1987) Cocrystals of yeast cytochrome c peroxidase and horse heart cytochrome c. J. Biol. Chem. 262, 13881-13884.
  160. Poulos, T.L., Edwards, S.L., Wariishi, H. and Gold, M.H. (1993) Crystallographic refinement of lignin peroxidase at 2 Å. J. Biol. Chem. 268, 4429-4440.
  161. Poulos, T.L., Patterson, W.R. and Sundaramoorthy, M. (1995) The crystal structure of ascorbate and manganese peroxidases: the role of non­haem metal in the catalytic mechanism. Biochem. Soc. Trans. 23, 228-232.
  162. Reading, N.S. and Aust, S.D. (1998) Effect of modified hemes on the spectral properties and activity of manganese peroxidase. Arch. Biochem. Biophys. 359, 291-296.
  163. Remba, R.D., Champion, P.M., Fitchen, D.B., Chiang, R. and Hager, L.P. (1979) Resonance Raman investigations of chloroperoxidase, horseradish peroxidase, and cytochrome c using Soret band laser excitation. Biochemistry 18, 2280-2290.
  164. Roberts, J.E., Hoffman, B.M., Rutter, R. and Hager, L.P. (1981) Electron­nuclear double resonance of horseradish peroxidase compound I. Detection of the porphyrin pi­cation radical. J. Biol. Chem. 256, 2118-2121.
  165. Rodriguez­Lopez, J.N., Hernández­Ruiz, J., Garcia­Cánovas, F., Thorneley, R.N.F., Acosta, M. and Arnao, M.B. (1997) The inactivation and catalytic pathways of horseradish peroxidase with m­chloroperoxybenzoic acid: A spectrophotometric and transient kinetic study. J. Biol. Chem. 272, 5469-5476.
  166. Rodriguez­Lopez, J.N., George, S.J. and Thorneley, R.N.F. (1998) The structure of carbonyl horseradish peroxidase: spectroscopic and kinetic characterization of the carbon monoxide complexes of His­42->Leu and Arg­38->Leu mutants. J. Biol. Inorg. Chem. 3, 44-52.
  167. Rodriguez­Maranon, M.J., Stillman, M.J. and van Huystee, R.B. (1993) Co­dependency of calcium and porphyrin for an integrated molecular structure of peanut peroxidase: a circular dichroism analysis. Biochem. Biophys. Res. Commun. 194, 326-332.
  168. Rodriguez­Maranon, M.J., Mercier, D., van Huystee, R.B. and Stillman, M.J. (1994) Analysis of the optical absorption and magnetic­circular­dichroism spectra of peanut peroxidase: electronic structure of a peroxidase with biochemical properties similar to those of horseradish peroxidase. Biochem. J. 301, 335-341.
  169. Rutter, R., Valentine, M., Hendrich, M.P., Hager, L.P. and Debrunner, P.G. (1983) Chemical nature of the porphyrin pi cation radical in horseradish peroxidase compound I. Biochemistry 22, 4769-4774.
  170. Sakurada, J., Takahashi, S. and Hosoya, T. (1986) Nuclear magnetic resonance studies on the spatial relationship of aromatic donor molecules to the heme iron of horseradish peroxidase. J. Biol. Chem. 261, 9657-9662.
  171. Satterlee, J.D. and Erman, J.E. (1981) Proton nuclear magnetic resonance characterization of the oxidized intermediates of cytochrome c peroxidase. J. Biol. Chem. 256, 1091-1093.
  172. Satterlee, J.D. and Erman, J.E. (1983) Deuterium exchangeable proton hyperfine resonances of low­spin cytochrome c peroxidase and the mechanism of peroxidase catalysis. Biochim. Biophys. Acta 743, 149-154.
  173. Satterlee, J.D., Erman, J.E., La Mar, G.N., Smith, K.M. and Langry, K.C. (1983) Assignment of hyperfine shifted resonances in high­spin forms of cytochrome c peroxidase by reconstitutions with deuterated hemins. Biochim. Biophys. Acta 743, 246-255.
  174. Satterlee, J.D., Erman, J.E. and de Ropp, J.S. (1987a) Proton hyperfine resonance assignments in cyanide­ligated cytochrome c peroxidase using the nuclear Overhauser effect. J. Biol. Chem. 262, 11578-11583.
  175. Satterlee, J.D., Moench, S.J. and Erman, J.E. (1987b) A proton NMR study of the non­covalent complex of horse cytochrome c and yeast cytochrome­c peroxidase and its comparison with other interacting protein complexes. Biochim. Biophys. Acta 912, 87-97.
  176. Satterlee, J.D., Erman, J.E., Mauro, J.M. and Kraut, J. (1990) Comparative proton NMR analysis of wild­type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp­235->Asn­235 mutant. Biochemistry 29, 8797-8804.
  177. Satterlee, J.D., Alam, S.L., Mauro, J.M., Erman, J.E. and Poulos, T.L. (1994) The effect of the Asn82->Asp mutation in yeast cytochrome c peroxidase studied by proton NMR spectroscopy. Eur. J. Biochem. 224, 81-87.
  178. Schuller, D.J., Ban, N., van Huystee, R.B., McPherson, A. and Poulos, T.L. (1996) The crystal structure of peanut peroxidase. Structure 4, 311-321.
  179. 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.
  180. Shiro, Y., Kurono, M. and Morishima, I. (1986) Presence of endogenous calcium ion and its functional and structural regulation in horseradish peroxidase. J. Biol. Chem. 261, 9382-9390.
  181. Shiro, Y., Makino, R., Sato, F., Oyanagi, H., Matsushita, T., Ishimura, Y. and Iizuka, T. (1991) Structural and electronic characterization of heme moiety in oxygenated hemoproteins by using XANES spectroscopy. Biochim. Biophys. Acta 1115, 101-107.
  182. Sievers, G. (1978) Circular dichroism studies on cytochrome c peroxidase from baker's yeast (Saccharomyces cerevisiae). Biochim. Biophys. Acta 536, 212-225.
  183. Sievers, G., Osterlund, K. and Ellfolk, N. (1979) Resonance Raman study on yeast cytochrome c peroxidase. Effect of coordination and axial ligands. Biochim. Biophys. Acta 581, 1-14.
  184. Sinclair, R., Yamazaki, I., Bumpus, J., Brock, B., Chang, C.S., Albo, A. and Powers, L. (1992) Structure of the active site of lignin peroxidase isozyme H2: native enzyme, compound III, and reduced form. Biochemistry 31, 4892-4900.
  185. Sinclair, R., Copeland, B., Yamazaki, I. and Powers, L. (1995) X­ray absorption spectroscopy comparison of the active site structures of Phanerochaete chrysosporium lignin peroxidase isoenzymes H2, H3, H4, H5, H8, and H10. Biochemistry 34, 13176-13182.
  186. Sinclair, R., Hallam, S., Chen, M., Chance, B. and Powers, L. (1996) Active site structure in cytochrome c peroxidase and myoglobin mutants: Effects of altered hydrogen bonding to the proximal histidine. Biochemistry 35, 15120-15128.
  187. Sitter, A.J., Reczek, C.M. and Terner, J. (1985) Heme­linked ionization of horseradish peroxidase compound II monitored by the resonance Raman Fe(IV)=O stretching vibration. J. Biol. Chem. 260, 7515-7522.
  188. Sitter, A.J., Shifflett, J.R. and Terner, J. (1988) Resonance Raman spectroscopic evidence for heme iron­hydroxide ligation in peroxidase alkaline forms. J. Biol. Chem. 263, 13032-13038.
  189. Sivaraja, M., Goodin, D.B., Smith, M. and Hoffman, B.M. (1989) Identification by ENDOR of Trp191 as the free­radical site in cytochrome c peroxidase compound ES. Science 245, 738-740.
  190. Smith, M.B. and Millett, F. (1980) A 19F nuclear magnetic resonance study of the interaction between cytochrome c and cytochrome c peroxidase. Biochim. Biophys. Acta 626, 64-72.
  191. Smulevich, G. and Spiro, T.G. (1985) Nanosecond transient resonance Raman spectra of the FeII-CO and FeIII-NO photolysis products of horseradish peroxidase. Biochim. Biophys. Acta 830, 80-85.
  192. Smulevich, G., Dasgupta, S., English, A.M. and Spiro, T.G. (1986a) Transient resonance Raman spectroscopy shows unrelaxed heme following CO photodissociation from cytochrome­c peroxidase. Biochim. Biophys. Acta 873, 88-91.
  193. Smulevich, G., Evangelista­Kirkup, R., English, A.M. and Spiro, T.G. (1986b) Raman and infrared spectra of cytochrome c peroxidase-carbon monoxide adducts in alternative conformational states. Biochemistry 25, 4426-4430.
  194. Smulevich, G., Mauro, J.M., Fishel, L.A., English, A.M., Kraut, J. and Spiro, T.G. (1988a) Heme pocket interactions in cytochrome c peroxidase studied by site­directed mutagenesis and resonance Raman spectroscopy. Biochemistry 27, 5477-5485.
  195. Smulevich, G., Mauro, J.M., Fishel, L.A., English, A.M., Kraut, J. and Spiro, T.G. (1988b) Cytochrome c peroxidase mutant active site structures probed by resonance Raman and infrared signatures of the CO adducts. Biochemistry 27, 5486-5492.
  196. Smulevich, G., Mantini, A.R., English, A.M. and Mauro, J.M. (1989a) Effects of temperature and glycerol on the resonance Raman spectra of cytochrome c peroxidase and selected mutants. Biochemistry 28, 5058-5064.
  197. Smulevich, G., Miller, M.A., Gosztola, D. and Spiro, T.G. (1989b) Photodissociable endogenous ligand in alkaline­reduced cytochrome c peroxidase implicates distal protein tension. Biochemistry 28, 9905-9908.
  198. Smulevich, G., Wang, Y., Mauro, J.M., Wang, J.M., Fishel, L.A., Kraut, J. and Spiro, T.G. (1990a) Single­crystal resonance Raman spectroscopy of site­directed mutants of cytochrome c peroxidase. Biochemistry 29, 7174-7180.
  199. Smulevich, G., Wang, Y., Edwards, S.L., Poulos, T.L., English, A.M. and Spiro, T.G. (1990b) Resonance Raman spectroscopy of cytochrome c peroxidase single crystals on a variable­temperature microscope stage. Biochemistry 29, 2586-2592.
  200. Smulevich, G., English, A.M., Mantini, A.R. and Marzocchi, M.P. (1991a) Resonance Raman investigation of ferric iron in horseradish peroxidase and its aromatic donor complexes at room and low temperatures. Biochemistry 30, 772-779.
  201. Smulevich, G., Miller, M.A., Kraut, J. and Spiro, T.G. (1991b) Conformational change and histidine control of heme chemistry in cytochrome c peroxidase: Resonance Raman evidence from Leu­52 and Gly­181 mutants of cytochrome c peroxidase. Biochemistry 30, 9546-9558.
  202. Smulevich, G., Paoli, M., Burke, J.F., Sanders, S.A., Thorneley, R.N.F. and Smith, A.T. (1994a) Characterization of recombinant horseradish peroxidase C and three site­directed mutants, F41V, F41W, and R38K, by resonance Raman spectroscopy. Biochemistry 33, 7398-7407.
  203. Smulevich, G., Feis, A., Focardi, C., Tams, J. and Welinder, K.G. (1994b) Resonance Raman study of the active site of Coprinus cinereus peroxidase. Biochemistry 33, 15425-15432.
  204. Smulevich, G., Neri, F., Willemsen, O., Choudhury, K., Marzocchi, M.P. and Poulos, T.L. (1995) Effect of the His175->Glu mutation on the heme pocket architecture of cytochrome c peroxidase. Biochemistry 34, 13485-13490.
  205. Smulevich, G., Neri, F., Marzocchi, M.P. and Welinder, K.G. (1996) Versatility of heme coordination demonstrated in a fungal peroxidase. Absorption and resonance Raman studies of Coprinus cinereus peroxidase and the Asp245->Asn mutant at various pH values. Biochemistry 35, 10576-10585.
  206. Smulevich, G., Paoli, M., De Sanctis, G., Mantini, A.R., Ascoli, F. and Coletta, M. (1997) Spectroscopic evidence for a conformational transition in horseradish peroxidase at very low pH. Biochemistry 36, 640-649.
  207. Smulevich, G., Feis, A., Indiani, C., Becucci, M. and Marzocchi, M.P. (1999) Peroxidase-benzhydroxamic acid complexes: spectroscopic evidence that a Fe-H2O distance of 2.6 Å can correspond to hexa­coordinate high­spin heme. J. Biol. Inorg. Chem. 4, 39-47.
  208. Spiro, T.G., Smulevich, G. and Su, C. (1990) Probing protein structure and dynamics with resonance Raman spectroscopy: cytochrome c peroxidase and hemoglobin. Biochemistry 29, 4497-4508.
  209. Su, X.D., Yonetani, T. and Skoglund, U. (1994) The crystal structure of the iron­free cytochrome c peroxidase and its implication for the enzymatic mechanism. FEBS Lett. 351, 437-442.
  210. Sun, J., Fitzgerald, M.M., Goodin, D.B. and Loehr, T.M. (1997) Solution and crystal structures of the H175G mutant of cytochrome c peroxidase: A resonance Raman study. J. Am. Chem. Soc. 119, 2064-2065.
  211. Sundaramoorthy, M., Choudhury, K., Edwards, S.L. and Poulos, T.L. (1991) Crystal structure and preliminary functional analysis of the cytochrome c peroxidase His175Gln proximal ligand mutant. J. Am. Chem. Soc. 113, 7755-7757.
  212. Sundaramoorthy, M., Kishi, K., Gold, M.H. and Poulos, T.L. (1994a) Preliminary crystallographic analysis of manganese peroxidase from Phanerochaete chrysosporium. J. Mol. Biol. 238, 845-848.
  213. Sundaramoorthy, M., Kishi, K., Gold, M.H. and Poulos, T.L. (1994b) The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06­Å resolution. J. Biol. Chem. 269, 32759-32767.
  214. Sundaramoorthy, M., Kishi, K., Gold, M.H. and Poulos, T.L. (1997) Crystal structures of substrate binding site mutants of manganese peroxidase. J. Biol. Chem. 272, 17574-17580.
  215. Sutherland, G.R.J. and Aust, S.D. (1997) Thermodynamics of binding of the distal calcium to manganese peroxidase. Biochemistry 36, 8567-8573.
  216. Sutherland, G.R.J., Zapanta, L.S., Tien, M. and Aust, S.D. (1997) Role of calcium in maintaining the heme environment of manganese peroxidase. Biochemistry 36, 3654-3662.
  217. Tanaka, M., Nagano, S., Ishimori, K. and Morishima, I. (1997a) Hydrogen bond network in the distal site of peroxidases: Spectroscopic properties of Asn70->Asp horseradish peroxidase mutant. Biochemistry 36, 9791-9798.
  218. Tanaka, M., Ishimori, K., Mukai, M., Kitagawa, T. and Morishima, I. (1997b) Catalytic activities and structural properties of horseradish peroxidase distal His42->Glu or Gln mutant. Biochemistry 36, 9889-9898.
  219. Taraban, M.B., Leshina, T.V., Anderson, M.A. and Grissom, C.B. (1997) Magnetic field dependence of electron transfer and the role of electron spin in heme enzymes: Horseradish peroxidase. J. Am. Chem. Soc. 119, 5768-5769.
  220. Thanabal, V., La Mar, G.N. and de Ropp, J.S. (1988) A nuclear Overhauser effect study of the heme crevice in the resting state and compound I of horseradish peroxidase: evidence for cation radical delocalization to the proximal histidine. Biochemistry 27, 5400-5407.
  221. Timofeevski, S.L. and Aust, S.D. (1997) Kinetics of calcium release from manganese peroxidase during thermal inactivation. Arch. Biochem. Biophys. 342, 169-175.
  222. Turano, P., Ferrer, J.C., Cheesman, M.R., Thomson, A.J., Banci, L., Bertini, I. and Mauk, A.G. (1995) pH, electrolyte, and substrate­linked variation in active site structure of the Trp51Ala variant of cytochrome c peroxidase. Biochemistry 34, 13895-13905.
  223. Veitch, N.C. and Williams, R.J.P. (1990) Two­dimensional 1H­NMR studies of horseradish peroxidase C and its interaction with indole­3­propionic acid. Eur. J. Biochem. 189, 351-362.
  224. Veitch, N.C. and Williams, R.J.P. (1995) The use of methyl­substituted benzhydroxamic acids as structural probes of peroxidase substrate binding. Eur. J. Biochem. 229, 629-640.
  225. Veitch, N.C., Williams, R.J.P., Bray, R.C., Burke, J.F., Sanders, S.A., Thorneley, R.N.F. and Smith, A.T. (1992a) Structural studies by proton­NMR spectroscopy of plant horseradish peroxidase C, the wild­type recombinant protein from Escherichia coli and two protein variants, Phe41->Val and Arg38->Lys. Eur. J. Biochem. 207, 521-531.
  226. Veitch, N.C., Williams, R.J.P., Smith, A.T., Sanders, S.A., Thorneley, R.N.F., Bray, R.C. and Burke, J.F. (1992b) Investigation of native and mutant plant peroxidases by NMR spectroscopy. Biochem. Soc. Trans. 20, 114S.
  227. Veitch, N.C., Tams, J.W., Vind, J., Dalboge, H. and Welinder, K.G. (1994) NMR studies of recombinant Coprinus peroxidase and three site­directed mutants. Implications for peroxidase substrate binding. Eur. J. Biochem. 222, 909-918.
  228. Veitch, N.C., Williams, R.J.P., Bone, N.M., Burke, J.F. and Smith, A.T. (1995) Solution characterisation by NMR spectroscopy of two horseradish peroxidase isoenzyme C mutants with alanine replacing either Phe142 or Phe143. Eur. J. Biochem. 233, 650-658.
  229. Veitch, N.C., Gao, Y. and Welinder, K.G. (1996) The Asp245->Asn mutant of Coprinus cinereus peroxidase. Characterization by 1H­NMR spectroscopy and comparison with the wild­type enzyme. Biochemistry 35, 14370-14380.
  230. Veitch, N.C., Gao, Y., Smith, A.T. and White, C.G. (1997) Identification of a critical phenylalanine residue in horseradish peroxidase, Phe179, by site­directed mutagenesis and 1H­NMR: Implications for complex formation with aromatic donor molecules. Biochemistry 36, 14751-14761.
  231. Vitello, L.B., Erman, J.E., Miller, M.A., Wang, J. and Kraut, J. (1993) Effect of arginine­48 replacement on the reaction between cytochrome c peroxidase and hydrogen peroxide. Biochemistry 32, 9807-9818.
  232. Wang, J., Larsen, R.W., Moench, S.J., Satterlee, J.D., Rousseau, D.L. and Ondrias, M.R. (1996) Cytochrome c peroxidase complexed with cytochrome c has an unperturbed heme moiety. Biochemistry 35, 453-463.
  233. Wang, J.M., Mauro, J.M., Edwards, S.L., Oatley, S.J., Fishel, L.A., Ashford, V.A., Xuong, N.­H. and Kraut, J. (1990) X­ray structures of recombinant yeast cytochrome c peroxidase and three heme­cleft mutants prepared by site­directed mutagenesis. Biochemistry 29, 7160-7173.
  234. Wang, K., Mei, H., Geren, L., Miller, M.A., Saunders, A., Wang, X., Waldner, J.L., Pielak, G.J., Durham, B. and Millett, F. (1996) Design of a ruthenium­cytochrome c derivative to measure electron transfer to the radical cation and oxyferryl heme in cytochrome c peroxidase. Biochemistry 35, 15107-15119.
  235. Wilcox, S.K., Jensen, G.M., Fitzgerald, M.M., McRee, D.E. and Goodin, D.B. (1996) Altering substrate specificity at the heme edge of cytochrome c peroxidase. Biochemistry 35, 4858-4866.
  236. Wilcox, S.K., Putnam, C.D., Sastry, M., Blankenship, J., Chazin, W.J., McRee, D.E. and Goodin, D.B. (1998) Rational design of a functional metalloenzyme: introduction of a site for manganese binding and oxidation into a heme peroxidase. Biochemistry 37, 16853-16862.
  237. Williams, R.J.P., Wright, P.E., Mazza, G. and Ricard, J.R. (1975) Proton magnetic resonance studies of peroxidases from turnip and horseradish. Biochim. Biophys. Acta 412, 127-147.
  238. Yeung, B.K.S., Wang, X., Sigman, J.A., Petillo, P.A. and Lu, Y. (1997) Construction and characterization of a manganese­binding site in cytochrome c peroxidase: towards a novel manganese peroxidase. Chemistry & Biology 4, 215-221.
  239. Yi, Q., Erman, J.E. and Satterlee, J.D. (1993) Proton NMR studies of noncovalent complexes of cytochrome c peroxidase­cyanide with horse and yeast ferricytochromes c. Biochemistry 32, 10988-10994.
  240. Youn, H.­D., Yim, Y.I, Kim K, Hah, Y.C. and Kang, S.­O. (1995) Spectral characterization and chemical modification of catalase­peroxidase from Streptomyces sp. J. Biol. Chem. 270, 13740-13747.
  241. Zimmer, J. and van Wart, H.E. (1982) Resonance Raman spectrum of horseradish peroxidase compound III: comparison with oxyhemoglobin. Biochem. Biophys. Res. Commun. 108, 977-981.
Reviews on fungal, plant and bacterial haem peroxidases