TSRI's main web site PROMISE mirror at TSRI Metalloprotein DB site Created: 17 June 1996
Last modified: 16 April 1999

Bibliography on structural studies of Class I cytochromes c

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  1. Aasa, R., Ellfolk, N., Ronnberg, M. and Vänngård, T. (1981) Electron paramagnetic resonance studies of Pseudomonas cytochrome c peroxidase. Biochim. Biophys. Acta 670, 170-175.
  2. Adir, N., Axelrod, H.L., Beroza, P., Isaacson, R.A., Rongey, S.H., Okamura, M.Y. and Feher, G. (1996) Co­crystallization and characterization of the photosynthetic reaction center­cytochrome c2 complex from Rhodobacter sphaeroides. Biochemistry 35, 2535-2547.
  3. Albert, I., Rutherford, A.W., Grav, H., Kellermann, J. and Michel, H. (1998) The 18 kDa cytochrome c553 from Heliobacterium gestii: Gene sequence and characterization of the mature protein. Biochemistry 37, 9001-9008.
  4. Almassy, R.J. and Dickerson, R.E. (1978) Pseudomonas cytochrome c551 at 2.0 Å resolution: enlargement of the cytochrome c family. Proc. Natl. Acad. Sci. USA 75, 2674-2678.
  5. Ashida, T., Ueki, T., Tsukihara, T., Sugihara, A. and Takano, T. (1971) The crystal structure of Bonito (Katsuo) ferrocytochrome c at 4 Å resolution. J. Biochem. (Tokyo) 70, 913-924.
  6. Auld, D.S., Young, G.B., Saunders, A.J., Doyle, D.F., Betz, S.F. and Pielak, G.J. (1993) Probing weakly polar interactions in cytochrome c. Protein Science 2, 2187-2197.
  7. Axelrod, H.L., Feher, G., Allen, J.P., Chirino, A.J., Day, M.W., Hsu, B.T. and Rees, D.C. (1994) Crystallization and X­ray structure determination of cytochrome c2 from Rhodobacter sphaeroides in three crystal forms. Acta Crystallogr. D50, 596-602.
  8. Bai, Y., Milne, J.S., Mayne, L. and Englander, S.W. (1994) Protein stability parameters measured by hydrogen exchange. Proteins 20, 4-14.
  9. Bai, Y., Sosnick, T.R., Mayne, L. and Englander, S.W. (1995) Protein folding intermediates: native­state hydrogen exchange. Science 269, 192-197.
  10. Baistrocchi, P., Banci, L., Bertini, I., Turano, P., Bren, K.L. and Gray, H.B. (1996) Three­dimensional solution structure of Saccharomyces cerevisiae reduced iso­1­cytochrome c. Biochemistry 35, 13788-13796.
  11. Banci, L., Bertini, I., Bren, K.L., Gray, H.B. and Turano, P. (1995a) pH­Dependent equilibria of yeast Met80Ala­iso­1­cytochrome c probed by NMR spectroscopy: A comparison with the wild­type protein. Chemistry & Biology 2, 377-383.
  12. Banci, L., Bertini, I., Bren, K.L., Gray, H.B., Sompornpisut, P. and Turano, P. (1995b) Three­dimensional solution structure of the cyanide adduct of a Met80Ala variant of Saccharomyces cerevisiae iso­1­cytochrome c. Identification of ligand­residue interactions in the distal heme cavity. Biochemistry 34, 11385-11398.
  13. Banci, L., Bertini, I., Bren, K.L., Cremonini, M.A., Gray, H.B., Luchinat, C. and Turano, P. (1996a) The use of pseudocontact shifts to refine solution structures of paramagnetic metalloproteins: Met80Ala cyano­cytochrome c as an example. J. Biol. Inorg. Chem. 1, 117-126.
  14. Banci, L., Bertini, I., Quacquarini, G., Walter, O., Díaz, A., Hervás, M. and de la Rosa, M.A. (1996b) The solution structure of cytochrome c6 from the green alga Monoraphidium braunii. J. Biol. Inorg. Chem. 1, 330-340.
  15. Banci, L., Bertini, I., Bren, K.L., Gray, H.B., Sompornpisut, P. and Turano, P. (1997a) Solution structure of oxidized Saccharomyces cerevisiae iso­1­cytochrome c. Biochemistry 36, 8992-9001.
  16. Banci, L., Bertini, I., Gray, H.B., Luchinat, C., Reddig, T., Rosato, A. and Turano, P. (1997b) Solution structure of oxidized horse heart cytochrome c. Biochemistry 36, 9867-9877.
  17. Banci, L., Bertini, I., Savellini, G.G., Romagnoli, A., Turano, P., Cremonini, M.A., Luchinat, C. and Gray, H.B. (1997c) Pseudocontact shifts as constraints for energy minimization and molecular dynamics calculations on solution structures of paramagnetic metalloproteins. Proteins 29, 68-76.
  18. Banci, L., Bertini, I., de la Rosa, M.A., Koulougliotis, D., Navarro, J.A. and Walter, O. (1998a) Solution structure of oxidized cytochrome c6 from the green alga Monoraphidium braunii. Biochemistry 37, 4831-4843.
  19. Banci, L., Bertini, I., Spyroulias, G.A. and Turano, P. (1998b) The conformational flexibility of oxidized cytochrome c studied through its interaction with NH3 and at high temperatures. Eur. J. Inorg. Chem., 583-591.
  20. Banci, L., Bertini, I., Reddig, T. and Turano, P. (1998c) Monitoring the conformational flexibility of cytochrome c at low ionic strength by 1H­NMR spectroscopy. Eur. J. Biochem. 256, 271-278.
  21. Banci, L., Bertini, I., Luchinat, C., Pierattelli, R., Shokhirev, N.V. and Walker, F.A. (1998d) Analysis of the temperature dependence of the 1H and 13C isotropic shifts of horse heart ferricytochrome c: Explanation of Curie and anti­Curie temperature dependence and nonlinear pseudocontact shifts in a common two­level framework. J. Am. Chem. Soc. 120, 8472-8479.
  22. Banci, L., Bertini, I., Huber, J.G., Spyroulias, G.A. and Turano, P. (1999) Solution structure of reduced horse heart cytochrome c. J. Biol. Inorg. Chem. 4, 21-31. [Electronic Supplementary Material]
  23. Battistuzzi, G., Borsari, M., Ferretti, S., Sola, M. and Soliani, E. (1995a) Cyclic voltammetry and 1H­NMR of Rhodopseudomonas palustris cytochrome c2 pH­dependent conformational states. Eur. J. Biochem. 232, 206-213.
  24. Battistuzzi, G., Borsari, M., Dallari, D., Ferretti, S. and Sola, M. (1995b) Cyclic voltammetry and 1H­NMR of Rhodopseudomonas palustris cytochrome c2. Probing surface charges through anion­binding studies. Eur. J. Biochem. 233, 335-339.
  25. Battistuzzi, G., Borsari, M., Dallari, D., Lancellotti, I. and Sola, M. (1996) Anion binding to mitochondrial cytochromes c studied through electrochemistry. Effects of the neutralization of surface charges on the redox potential. Eur. J. Biochem. 241, 208-214.
  26. Battistuzzi, G., Borsari, M., Sola, M. and Francia, F. (1997) Redox thermodynamics of the native and alkaline forms of eukaryotic and bacterial class I cytochromes c. Biochemistry 36, 16247-16258.
  27. Baxter, S.M. and Fetrow, J.S. (1999) Hydrogen exchange behavior of [U-15N]­labeled oxidized and reduced iso­1­cytochrome c. Biochemistry 38, 4493-4503. [Electronic Supplementary Material]
  28. Baxter, S.M., Boose, T.L. and Fetrow, J.S. (1997) 15N isotopic labeling and amide hydrogen exchange rates of oxidized iso­1­cytochrome c. J. Am. Chem. Soc. 119, 9899-9900.
  29. Behere, D.V., Ales, D.C. and Goff, H.M. (1986) Proton and nitrogen­15 NMR studies of ferricytochrome c cyanide complexes: remarkable conservation of the heme environment among organisms of diverse origin. Biochim. Biophys. Acta 871, 285-292.
  30. Beissinger, M., Sticht, H., Sutter, M., Ejchart, A., Haehnel, W. and Rosch, P. (1998) Solution structure of cytochrome c6 from the thermophilic cyanobacterium Synechococcus elongatus. EMBO J. 17, 27-36.
  31. Benini, S., Ciurli, S., Rypniewski, W.R. and Wilson, K.S. (1997) Crystals of cytochrome c553 from Bacillus pasteurii show diffraction to 0.97 Å resolution. Proteins 28, 580-585.
  32. Benini, S., Borsari, M., Ciurli, S., Dikiy, A. and Lamborghini, M. (1998) Modulation of Bacillus pasteurii cytochrome c553 reduction potential by structural and solution parameters. J. Biol. Inorg. Chem. 3, 371-382.
  33. Benning, M.M., Wesenberg, G., Caffrey, M.S., Bartsch, R.G., Meyer, T.E., Cusanovich, M.A., Rayment, I. and Holden, H.M. (1991) Molecular structure of cytochrome c2 isolated from Rhodobacter capsulatus determined at 2.5 Å resolution. J. Mol. Biol. 220, 673-685.
  34. Benning, M.M., Meyer, T.E. and Holden, H.M. (1994) X­ray structure of the cytochrome c2 isolated from Paracoccus denitrificans refined to 1.7­Å resolution. Arch. Biochem. Biophys. 310, 460-466.
  35. Benning, M.M., Meyer, T.E. and Holden, H.M. (1996) Molecular structure of a high potential cytochrome c2 isolated from Rhodopila globiformis. Arch. Biochem. Biophys. 333, 338-348.
  36. Berghuis, A.M. and Brayer, G.D. (1992) Oxidation state­dependent conformational changes in cytochrome c. J. Mol. Biol. 223, 959-976.
  37. Berghuis, A.M., Guillemette, J.G., Smith, M. and Brayer, G.D. (1994a) Mutation of tyrosine­67 to phenylalanine in cytochrome c significantly alters the local heme environment. J. Mol. Biol. 235, 1326-1341.
  38. Berghuis, A.M., Guillemette, J.G., McLendon, G., Sherman, F., Smith, M. and Brayer, G.D. (1994b) The role of a conserved internal water molecule and its associated hydrogen bond network in cytochrome c. J. Mol. Biol. 236, 786-799.
  39. Bersch, B., Brutscher, B., Meyer, T.E. and Marion, D. (1995) 1H and 13C NMR assignments and structural aspects of a ferrocytochrome c551 from the purple phototrophic bacterium Ectothiorhodospira halophila. Eur. J. Biochem. 227, 249-260.
  40. Bersch, B., Blackledge, M.J., Meyer, T.E. and Marion, D. (1996) Ectothiorhodospira halophila ferrocytochrome c551: Solution structure and comparison with bacterial cytochromes c. J. Mol. Biol. 264, 567-584.
  41. Bhuyan, A.K. and Udgaonkar, J.B. (1998) Multiple kinetic intermediates accumulate during the unfolding of horse cytochrome c in the oxidized state. Biochemistry 37, 9147-9155.
  42. Blanchard, L., Marion, D., Pollock, B., Voordouw, G., Wall, J., Bruschi, M. and Guerlesquin, F. (1993) Overexpression of Desulfovibrio vulgaris Hildenborough cytochrome c553 in Desulfovibrio desulfuricans G200. Evidence of conformational heterogeneity in the oxidized protein by NMR. Eur. J. Biochem. 218, 293-301.
  43. Blanchard, L., Dolla, A., Bersch, B., Forest, E., Bianco, P., Wall, J., Marion, D. and Guerlesquin, F. (1994) Effects of the Tyr64 substitution on the stability of cytochrome c553, a low oxidoreduction­potential cytochrome from Desulfovibrio vulgaris Hildenborough. Eur. J. Biochem. 226, 423-432.
  44. Blanchard, L., Blackledge, M.J., Marion, D. and Guerlesquin, F. (1996) Investigation of oxidation state­dependent conformational changes in Desulfovibrio vulgaris Hildenborough cytochrome c553 by two­dimensional 1H­NMR spectra. FEBS Lett. 389, 203-209.
  45. Blanchard, L., Hunter, C.N. and Williamson, M.P. (1997) The effect of ring currents on carbon chemical shift in cytochromes. J. Biomol. NMR 9, 389-395.
  46. 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.
  47. Boswell, A.P., McClune, G.J., Moore, G.R., Williams, R.J.P., Pettigrew, G.W., Inubishi, T., Yonetani, T. and Harris, D.E. (1980a) Nuclear­magnetic­resonance study of the interaction of cytochrome c with cytochrome c peroxidase. Biochem. Soc. Trans. 8, 637-638.
  48. Boswell, A.P., Moore, G.R., Williams, R.J.P., Chien, J.C. and Dickinson, L.C. (1980b) Nuclear magnetic resonance studies of the phenylalanine residues of eukaryotic cytochrome c. J. Inorg. Biochem. 13, 347-352.
  49. Boswell, A.P., Eley, C.G., Moore, G.R., Robinson, M.N., Williams, G., Williams, R.J.P., Neupert, W.J. and Hennig, B. (1982) 1H NMR studies of eukaryotic cytochrome c. Resonance assignments and iron­hexacyanide­mediated electron exchange. Eur. J. Biochem. 124, 289-294.
  50. Boussaad, S., Dziri, L., Arechabaleta, R., Tao, N.J. and Leblanc, R.M. (1998) Electron­transfer properties of cytochrome c Langmuir-Blodgett films and interactions of cytochrome c with lipids. Langmuir 14, 6215-6219.
  51. Brennan, L. and Turner, D.L. (1997) Paramagnetic NMR shifts in cyanoferricytochrome c. Investigation of thermal stability and deviations from Curie law behaviour. Biochim. Biophys. Acta 1342, 1-12.
  52. Burch, A.M., Rigby, S.E., Funk, W.D., MacGillivray, R.T., Mauk, M.R., Mauk, A.G. and Moore, G.R. (1990) NMR characterization of surface interactions in the cytochrome b5-cytochrome c complex. Science 247, 831-833.
  53. Burns, P.D. and La Mar, G.N. (1981) Characterization of conformational heterogeneity in the heme pocket of ferricytochrome c using high field proton nuclear magnetic resonance spectroscopy. J. Biol. Chem. 256, 4934-4939.
  54. Bushnell, G.W., Louie, G.V. and Brayer, G.D. (1990) High­resolution three­dimensional structure of horse heart cytochrome c. J. Mol. Biol. 214, 585-595.
  55. Caffrey, M.S., Gooley, P.R., Zhao, D., Meyer, T.E., Cusanovich, M.A. and MacKenzie, N.E. (1997) The substitution of proline 35 by alanine in Rhodobacter capsulatus cytochrome cytochrome c2 affects the overall protein stability but not the alkaline transition. Protein Engineering 10, 77-80.
  56. Cai, M.L. and Timkovich, R. (1991) Proton resonance assignments for Pseudomonas aeruginosa ferrocytochrome c­551. Biochem. Biophys. Res. Commun. 178, 309-314.
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  60. Carter, D.C., Melis, K.A., O'Donnell, S.E., Burgess, B.K., Furey, W.F., Jr., Wang, B.­C. and Stout, C.D. (1985) Crystal structure of Azotobacter cytochrome c5 at 2.5 Å resolution. J. Mol. Biol. 184, 279-295.
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  66. Chi, Z. and Asher, S.A. (1998) UV Raman determination of the environment and solvent exposure of Tyr and Trp residues. J. Phys. Chem. B102, 9595-9602.
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