Mechanisms of the reactions of cytochrome c. Rate and equilibrium constants for ligand binding to horse heart ferricytochrome c.

Citations

1. Frederick AK, Thompson SL, Vakharia ZM, Cherney MM, Lei H, Evenson G, Bowler BE. Effect on intrinsic peroxidase activity of substituting coevolved residues from Ω-loop C of human cytochrome c into yeast iso-1-cytochrome c. J Inorg Biochem 2022 Jul;232:111819.
   doi: 10.1016/j.jinorgbio.2022.111819pubmed: 35428021google scholar: lookup
2. Deng Y, Zhong F, Alden SL, Hoke KR, Pletneva EV. The K79G Mutation Reshapes the Heme Crevice and Alters Redox Properties of Cytochrome c. Biochemistry 2018 Oct 9;57(40):5827-5840.
   doi: 10.1021/acs.biochem.8b00650pubmed: 30142276google scholar: lookup
3. Zhong F, Pletneva EV. Ligation and Reactivity of Methionine-Oxidized Cytochrome c. Inorg Chem 2018 May 21;57(10):5754-5766.
   doi: 10.1021/acs.inorgchem.8b00010pubmed: 29708337google scholar: lookup
4. Gu J, Shin DW, Pletneva EV. Remote Perturbations in Tertiary Contacts Trigger Ligation of Lysine to the Heme Iron in Cytochrome c. Biochemistry 2017 Jun 13;56(23):2950-2966.
   doi: 10.1021/acs.biochem.6b01187pubmed: 28474881google scholar: lookup
5. Karsisiotis AI, Deacon OM, Wilson MT, Macdonald C, Blumenschein TM, Moore GR, Worrall JA. Increased dynamics in the 40-57 Ω-loop of the G41S variant of human cytochrome c promote its pro-apoptotic conformation. Sci Rep 2016 Jul 27;6:30447.
   doi: 10.1038/srep30447pubmed: 27461282google scholar: lookup
6. Amacher JF, Zhong F, Lisi GP, Zhu MQ, Alden SL, Hoke KR, Madden DR, Pletneva EV. A Compact Structure of Cytochrome c Trapped in a Lysine-Ligated State: Loop Refolding and Functional Implications of a Conformational Switch. J Am Chem Soc 2015 Jul 8;137(26):8435-49.
   doi: 10.1021/jacs.5b01493pubmed: 26038984google scholar: lookup
7. Nugraheni AD, Nagao S, Yanagisawa S, Ogura T, Hirota S. Interaction of dimeric horse cytochrome c with cyanide ion. J Biol Inorg Chem 2013 Mar;18(3):383-90.
   doi: 10.1007/s00775-013-0982-8pubmed: 23412550google scholar: lookup
8. Levin BD, Can M, Bowman SE, Bren KL, Elliott SJ. Methionine ligand lability in bacterial monoheme cytochromes c: an electrochemical study. J Phys Chem B 2011 Oct 13;115(40):11718-26.
   doi: 10.1021/jp203292hpubmed: 21870858google scholar: lookup
9. Rajagopal BS, Wilson MT, Bendall DS, Howe CJ, Worrall JA. Structural and kinetic studies of imidazole binding to two members of the cytochrome c (6) family reveal an important role for a conserved heme pocket residue. J Biol Inorg Chem 2011 Apr;16(4):577-88.
   doi: 10.1007/s00775-011-0758-ypubmed: 21267610google scholar: lookup
10. Sedlák E, Fabian M, Robinson NC, Musatov A. Ferricytochrome c protects mitochondrial cytochrome c oxidase against hydrogen peroxide-induced oxidative damage. Free Radic Biol Med 2010 Nov 30;49(10):1574-81.
    doi: 10.1016/j.freeradbiomed.2010.08.019pubmed: 20801213google scholar: lookup
11. Kokhan O, Shinkarev VP, Wraight CA. Binding of imidazole to the heme of cytochrome c1 and inhibition of the bc1 complex from Rhodobacter sphaeroides: II. Kinetics and mechanism of binding. J Biol Chem 2010 Jul 16;285(29):22522-31.
    doi: 10.1074/jbc.M110.128082pubmed: 20448037google scholar: lookup
12. Kokhan O, Shinkarev VP, Wraight CA. Binding of imidazole to the heme of cytochrome c1 and inhibition of the bc1 complex from Rhodobacter sphaeroides: I. Equilibrium and modeling studies. J Biol Chem 2010 Jul 16;285(29):22513-21.
    doi: 10.1074/jbc.M110.128058pubmed: 20448035google scholar: lookup
13. Varhac R, Antalík M. Correlation of acid-induced conformational transition of ferricytochrome c with cyanide binding kinetics. J Biol Inorg Chem 2008 Jun;13(5):713-21.
    doi: 10.1007/s00775-008-0357-8pubmed: 18317818google scholar: lookup
14. Tomásková N, Varhac R, Zoldák G, Oleksáková L, Sedláková D, Sedlák E. Conformational stability and dynamics of cytochrome c affect its alkaline isomerization. J Biol Inorg Chem 2007 Feb;12(2):257-66.
    doi: 10.1007/s00775-006-0183-9pubmed: 17120073google scholar: lookup
15. Zhong L, Wen X, Rabinowitz TM, Russell BS, Karan EF, Bren KL. Heme axial methionine fluxionality in Hydrogenobacter thermophilus cytochrome c552. Proc Natl Acad Sci U S A 2004 Jun 8;101(23):8637-42.
    doi: 10.1073/pnas.0402033101pubmed: 15161973google scholar: lookup
16. Schejter A, Koshy TI, Luntz TL, Sanishvili R, Vig I, Margoliash E. Effects of mutating Asn-52 to isoleucine on the haem-linked properties of cytochrome c. Biochem J 1994 Aug 15;302 ( Pt 1)(Pt 1):95-101.
    doi: 10.1042/bj3020095pubmed: 8068029google scholar: lookup
17. Dreyer JL. Electron transfer in biological systems: an overview. Experientia 1984 Jul 15;40(7):653-75.
    doi: 10.1007/BF01949719pubmed: 6378653google scholar: lookup
18. Jones GD, Jones MG, Wilson MT, Brunori M, Colosimo A, Sarti P. Reactions of cytochrome c oxidase with sodium dithionite. Biochem J 1983 Jan 1;209(1):175-82.
    doi: 10.1042/bj2090175pubmed: 6303299google scholar: lookup
19. Saleem MM, Wilson MT. Kinetic studies on the reduction of cytochrome c. Reaction with dihydroxy conjugated compounds (catechols and quinols). Biochem J 1982 Mar 1;201(3):433-44.
    doi: 10.1042/bj2010433pubmed: 6284121google scholar: lookup
20. Brittain T, Wilson MT, Greenwood C. The reduction of carboxymethyl-cytochrome c by chromous ions. Biochem J 1974 Aug;141(2):455-61.
    doi: 10.1042/bj1410455pubmed: 4375979google scholar: lookup
21. Creutz C, Sutin N. Reduction of ferricytochrome c by dithionite ion: electron transfer by parallel adjacent and remote pathways. Proc Natl Acad Sci U S A 1973 Jun;70(6):1701-3.
    doi: 10.1073/pnas.70.6.1701pubmed: 4352650google scholar: lookup
22. Ellis JA, Cross AR, Jones OT. Studies on the electron-transfer mechanism of the human neutrophil NADPH oxidase. Biochem J 1989 Sep 1;262(2):575-9.
    doi: 10.1042/bj2620575pubmed: 2553003google scholar: lookup
23. Tonge P, Moore GR, Wharton CW. Fourier-transform infra-red studies of the alkaline isomerization of mitochondrial cytochrome c and the ionization of carboxylic acids. Biochem J 1989 Mar 1;258(2):599-605.
    doi: 10.1042/bj2580599pubmed: 2539813google scholar: lookup
24. Simionescu N, Siminoescu M, Palade GE. Permeability of muscle capillaries to small heme-peptides. Evidence for the existence of patent transendothelial channels. J Cell Biol 1975 Mar;64(3):586-607.
    doi: 10.1083/jcb.64.3.586pubmed: 239003google scholar: lookup
25. Greenwood C, Brittain T, Brunori M, Wilson MT. Chromous ion reduction of mammalian cytochrome oxidase and some of its derivatives. Biochem J 1977 Aug 1;165(2):413-6.
    doi: 10.1042/bj1650413pubmed: 200223google scholar: lookup
26. Brittain T, Greenwood C. Kinetic studies on [methionine sulphoxide] cytochrome c. Biochem J 1976 Dec 1;159(3):621-6.
    doi: 10.1042/bj1590621pubmed: 188410google scholar: lookup
27. José do Nascimento A, Hishida do Nascimento K. Kinetics of reaction of (nitrotyrosyl)cytochrome c with ligands. Biochem J 1976 Jul 1;157(1):217-20.
    doi: 10.1042/bj1570217pubmed: 183741google scholar: lookup
28. Al-Ayash AI, Wilson MT. The mechanism of reduction of single-site redox proteins by ascorbic acid. Biochem J 1979 Feb 1;177(2):641-8.
    doi: 10.1042/bj1770641pubmed: 35158google scholar: lookup