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. 1988 Oct 1;255(1):353–356.

The binding characteristics of the cytochrome c iron.

A Schejter 1, B Plotkin 1
PMCID: PMC1135229  PMID: 2848510

Abstract

A comparison of the binding properties of myoglobin and cytochrome c shows that the latter, in the reduced state, has an unusually large affinity for ligands, including thioethers. This explains the outstanding stability of the methionine-iron bond of ferrous cytochrome c, and results from the intrinsic ability of the cytochrome c iron to delocalize its electrons into orbitals of the sixth axial ligand.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Caughey W. S., Barlow C. H., O'Keeffe D. H., O'Toole M. C. Spectroscopic studies of cis and trans effects in hemes and hemins. Ann N Y Acad Sci. 1973;206:296–309. doi: 10.1111/j.1749-6632.1973.tb43218.x. [DOI] [PubMed] [Google Scholar]
  2. Cooke R., Debrunner P. Mössbauer studies of the iron atom in cytochrome c. J Chem Phys. 1968 May 15;48(10):4532–4537. doi: 10.1063/1.1668022. [DOI] [PubMed] [Google Scholar]
  3. Dickerson R. E., Takano T., Eisenberg D., Kallai O. B., Samson L., Cooper A., Margoliash E. Ferricytochrome c. I. General features of the horse and bonito proteins at 2.8 A resolution. J Biol Chem. 1971 Mar 10;246(5):1511–1535. [PubMed] [Google Scholar]
  4. Eaton W. A., Hochstrasser R. M. Electronic spectrum of single crystals of ferricytochrome-c. J Chem Phys. 1967 Apr 1;46(7):2533–2539. doi: 10.1063/1.1841081. [DOI] [PubMed] [Google Scholar]
  5. Ellis P. E., Jones R. D., Basolo F. Sulfur base ligation to iron(II) and cobalt(II) porphyrins. Proc Natl Acad Sci U S A. 1979 Nov;76(11):5418–5420. doi: 10.1073/pnas.76.11.5418. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fergusson J. E., Robinson W. T., Rodley G. A. Significance of the orientation of coordinated imidazole and benzimidazole groups in haemoprotein and vitamin B 12 structures. Aust J Biol Sci. 1972 Dec;25(6):1365–1371. doi: 10.1071/bi9721365. [DOI] [PubMed] [Google Scholar]
  7. Fermi G. Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2-5 A resolution: refinement of the atomic model. J Mol Biol. 1975 Sep 15;97(2):237–256. doi: 10.1016/s0022-2836(75)80037-4. [DOI] [PubMed] [Google Scholar]
  8. GEORGE P., SCHEJTER A. THE REACTIVITY OF FERROCYTOCHROME C WITH IRON-BINDING LIGANDS. J Biol Chem. 1964 May;239:1504–1508. [PubMed] [Google Scholar]
  9. GEORGE P., TSOU C. L. Reaction between hydrocyanic acid, cyanide ion and ferricytochrome c. Biochem J. 1952 Feb;50(4):440–448. doi: 10.1042/bj0500440. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Gelin B. R., Karplus M. Mechanism of tertiary structural change in hemoglobin. Proc Natl Acad Sci U S A. 1977 Mar;74(3):801–805. doi: 10.1073/pnas.74.3.801. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. George P., Glauser S. C., Schejter A. The reactivity of ferricytochrome c with ionic ligands. J Biol Chem. 1967 Apr 25;242(8):1690–1695. [PubMed] [Google Scholar]
  12. Lang G., Herbert D., Yonetani T. Mössbauer spectroscopy of cytochrome C. J Chem Phys. 1968 Jul 15;49(2):944–950. doi: 10.1063/1.1670164. [DOI] [PubMed] [Google Scholar]
  13. Margoliash E., Schejter A. Cytochrome c. Adv Protein Chem. 1966;21:113–286. doi: 10.1016/s0065-3233(08)60128-x. [DOI] [PubMed] [Google Scholar]
  14. Mathews F. S. The structure, function and evolution of cytochromes. Prog Biophys Mol Biol. 1985;45(1):1–56. doi: 10.1016/0079-6107(85)90004-5. [DOI] [PubMed] [Google Scholar]
  15. SCHEJTER A., GEORGE P. THE 695-MMM. BAND OF FERRICYTOCHROME C AND ITS RELATIONSHIP TO PROTEIN CONFORMATION. Biochemistry. 1964 Aug;3:1045–1049. doi: 10.1021/bi00896a006. [DOI] [PubMed] [Google Scholar]
  16. Salmeen I., Palmer G. Electron paramagnetic resonance of beef-heart ferricytochrome c. J Chem Phys. 1968 Mar 1;48(5):2049–2052. doi: 10.1063/1.1669014. [DOI] [PubMed] [Google Scholar]
  17. Schejter A., Aviram I. The effects of alkylation of methionyl residues on the properties of horse cytochrome c. J Biol Chem. 1970 Apr 10;245(7):1552–1557. [PubMed] [Google Scholar]
  18. Schejter A., Aviram I. The reaction of cytochrome c with imidazole. Biochemistry. 1969 Jan;8(1):149–153. doi: 10.1021/bi00829a021. [DOI] [PubMed] [Google Scholar]
  19. Takano T., Dickerson R. E. Conformation change of cytochrome c. I. Ferrocytochrome c structure refined at 1.5 A resolution. J Mol Biol. 1981 Nov 25;153(1):79–94. doi: 10.1016/0022-2836(81)90528-3. [DOI] [PubMed] [Google Scholar]
  20. Takano T., Dickerson R. E. Conformation change of cytochrome c. II. Ferricytochrome c refinement at 1.8 A and comparison with the ferrocytochrome structure. J Mol Biol. 1981 Nov 25;153(1):95–115. doi: 10.1016/0022-2836(81)90529-5. [DOI] [PubMed] [Google Scholar]
  21. Wittenberg J. B., Wittenberg B. A. Preparation of myoglobins. Methods Enzymol. 1981;76:29–42. doi: 10.1016/0076-6879(81)76112-3. [DOI] [PubMed] [Google Scholar]
  22. Wüthrich K., Aviram I., Schejter A. Structural studies of modified cytochromes c by nuclear magnetic resonance spectroscopy. Biochim Biophys Acta. 1971 Nov 2;253(1):98–103. doi: 10.1016/0005-2728(71)90237-4. [DOI] [PubMed] [Google Scholar]

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