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Protein science : a publication of the Protein Society2006; 15(2); 234-241; doi: 10.1110/ps.051825906

The redox couple of the cytochrome c cyanide complex: the contribution of heme iron ligation to the structural stability, chemical reactivity, and physiological behavior of horse cytochrome c.

Abstract: Contrary to most heme proteins, ferrous cytochrome c does not bind ligands such as cyanide and CO. In order to quantify this observation, the redox potential of the ferric/ferrous cytochrome c-cyanide redox couple was determined for the first time by cyclic voltammetry. Its E0' was -240 mV versus SHE, equivalent to -23.2 kJ/mol. The entropy of reaction for the reduction of the cyanide complex was also determined. From a thermodynamic cycle that included this new value for the cyt c cyanide complex E0', the binding constant of cyanide to the reduced protein was estimated to be 4.7 x 10(-3) L M(-1) or 13.4 kJ/mol (3.2 kcal/mol), which is 48.1 kJ/mol (11.5 kcal/mol) less favorable than the binding of cyanide to ferricytochrome c. For coordination of cyanide to ferrocytochrome c, the entropy change was earlier experimentally evaluated as 92.4 J mol(-1) K(-1) (22.1 e.u.) at 25 K, and the enthalpy change for the same net reaction was calculated to be 41.0 kJ/mol (9.8 kcal/mol). By taking these results into account, it was discovered that the major obstacle to cyanide coordination to ferrocytochrome c is enthalpic, due to the greater compactness of the reduced molecule or, alternatively, to a lower rate of conformational fluctuation caused by solvation, electrostatic, and structural factors. The biophysical consequences of the large difference in the stabilities of the closed crevice structures are discussed.
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Publication Date: 2006-01-26 PubMed ID: 16434742PubMed Central: PMC2242453DOI: 10.1110/ps.051825906Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research study explores the chemical reactivity, structural stability, and physiological behavior of horse cytochrome c, focusing specifically on its interaction with cyanide. Unlike most heme proteins, which bind ligands such as cyanide and CO, ferrous cytochrome c does not. To explain and quantify this anomaly, the research outlines a thermodynamic cycle that includes the redox potential of the ferric/ferrous cytochrome c-cyanide redox couple.

Redox Potential Determination

  • The research started by determining the redox potential of the ferric/ferrous cytochrome c-cyanide redox couple. This involved applying cyclic voltammetry.
  • Eventually, it was found to be -240 mV versus SHE, the standard hydrogen electrode, equivalent to -23.2 kJ/mol.
  • This measurement made it possible to compare the redox potential of this specific redox couple to others.

Entropy of Reaction and Cyanide Binding Constant

  • The researchers also determined the entropy of reaction for the reduction of the cyanide complex.
  • Including this new value in a thermodynamic cycle, the cyanide binding constant to the reduced protein was estimated to be 4.7 x 10(-3) L M(-1) or 13.4 kJ/mol (3.2 kcal/mol).
  • Interestingly, this value is notably less favorable than the binding of cyanide to ferricytochrome c by 48.1 kJ/mol (11.5 kcal/mol).

Entropy Change and Enthalpy Change for Cyanide Coordination

  • For cyanide coordination to ferrocytochrome c, parameters such as the entropy change and enthalpy change were evaluated.
  • The entropy change was found to be 92.4 J mol(-1) K(-1) (22.1 e.u.) at 25 K, while the enthalpy change for the same net reaction was calculated to be 41.0 kJ/mol (9.8 kcal/mol).
  • These results revealed that the biggest barrier to cyanide coordination to ferrocytochrome c is enthalpic, resulting from the increased compactness of the reduced molecule or the reduced rate of conformational fluctuation caused by factors such as solvation, electrostatic, and structural elements.

Implications of Findings

  • The research also delved into the biophysical consequences of the significant difference in the stability of the closed crevice structures.
  • Understanding the behavior of cytochrome c can enhance our understanding of energy production in cells, and possibly find implication in the development of novel therapies for various diseases.

Cite This Article

APA
Schejter A, Ryan MD, Blizzard ER, Zhang C, Margoliash E, Feinberg BA. (2006). The redox couple of the cytochrome c cyanide complex: the contribution of heme iron ligation to the structural stability, chemical reactivity, and physiological behavior of horse cytochrome c. Protein Sci, 15(2), 234-241. https://doi.org/10.1110/ps.051825906

Publication

Protein science : a publication of the Protein Society
ISSN: 0961-8368
NlmUniqueID: 9211750
Country: United States
Language: English
Volume: 15
Issue: 2
Pages: 234-241

Researcher Affiliations

Schejter, Abel
  • Sackler Institute of Molecular Medicine, Sackler Medical School, Tel-Aviv University, Tel-Aviv 69978, Israel. molec03@post.tau.ac.il
Ryan, Michael D
    Blizzard, Erica R
      Zhang, Chongyao
        Margoliash, Emanuel
          Feinberg, Benjamin A

            MeSH Terms

            • Animals
            • Cyanides / metabolism
            • Cytochromes c / chemistry
            • Cytochromes c / metabolism
            • Entropy
            • Heme / metabolism
            • Horses
            • Iron / metabolism
            • Oxidation-Reduction
            • Protein Conformation
            • Static Electricity
            • Thermodynamics

            Grant Funding

            • GM 55892 / NIGMS NIH HHS

            References

            This article includes 36 references
            1. Balducci G, Costa G. The four-member square scheme in cyclic voltammetry: General solution for Nerstian electron transfers. J. Electroanal. Chem. 348: 355–365.
            2. Bard AJ, Faulkner LR. Electrochemical methods: Fundamentals and applications. .
            3. Bertrand P, Mbarki O, Asso M, Blanchard L, Guerlesquin F, Tegoni M. Control of the redox potential in c-type cytochromes: importance of the entropic contribution.. Biochemistry 1995 Sep 5;34(35):11071-9.
              pubmed: 7669764doi: 10.1021/bi00035a012google scholar: lookup
            4. Brautigan DL, Ferguson-Miller S, Margoliash E. Mitochondrial cytochrome c: preparation and activity of native and chemically modified cytochromes c.. Methods Enzymol 1978;53:128-64.
              pubmed: 213675doi: 10.1016/s0076-6879(78)53021-8google scholar: lookup
            5. Brayer GD, Murphy MEP. Structural studies of eukaryotic cytochromes c. In Cytochrome c—A multidisciplinary approach (eds. R.A. Scott and A. Grant Mauk), pp. 103–166.
            6. BUTT WD, KEILIN D. Absorption spectra and some other properties of cytochrome c and of its compounds with ligands.. Proc R Soc Lond B Biol Sci 1962 Nov 20;156:429-58.
              pubmed: 14040866doi: 10.1098/rspb.1962.0049google scholar: lookup
            7. Cohen DS, Pielak JG. Entropic stabilization of cytochrome c upon reduction. J. Am. Chem. Soc. 117: 1675–1677.
            8. Eden D, Matthew JB, Rosa JJ, Richards FM. Increase in apparent compressibility of cytochrome c upon oxidation.. Proc Natl Acad Sci U S A 1982 Feb;79(3):815-9.
              pmc: PMC345843pubmed: 6278497doi: 10.1073/pnas.79.3.815google scholar: lookup
            9. Evans DH. Solution electron-transfer reactions in organic and organometallic electrochemistry. Chem. Rev. 90: 739–751.
            10. Feinberg BA, Liu X, Ryan MD, Schejter A, Zhang C, Margoliash E. Direct voltammetric observation of redox driven changes in axial coordination and intramolecular rearrangement of the phenylalanine-82-histidine variant of yeast iso-1-cytochrome c.. Biochemistry 1998 Sep 22;37(38):13091-101.
              pubmed: 9748315doi: 10.1021/bi981037ngoogle scholar: lookup
            11. Fisher WR, Taniuchi H, Anfinsen CB. On the role of heme in the formation of the structure of cytochrome c.. J Biol Chem 1973 May 10;248(9):3188-95.
              pubmed: 4349479
            12. George P, Lyster RL. CREVICE STRUCTURES IN HEMOPROTEIN REACTIONS.. Proc Natl Acad Sci U S A 1958 Oct 15;44(10):1013-29.
              pmc: PMC528687pubmed: 16590301doi: 10.1073/pnas.44.10.1013google scholar: lookup
            13. GEORGE P, SCHEJTER A. THE REACTIVITY OF FERROCYTOCHROME C WITH IRON-BINDING LIGANDS.. J Biol Chem 1964 May;239:1504-8.
              pubmed: 14189884
            14. GEORGE P, TSOU CL. Reaction between hydrocyanic acid, cyanide ion and ferricytochrome c.. Biochem J 1952 Feb;50(4):440-8.
              pmc: PMC1197682pubmed: 14925115doi: 10.1042/bj0500440google scholar: lookup
            15. George P, Glauser SC, Schejter A. The reactivity of ferricytochrome c with ionic ligands.. J Biol Chem 1967 Apr 25;242(8):1690-5.
              pubmed: 6024762
            16. Harbury HA, Cronin JR, Fanger MW, Hettinger TP, Murphy AJ, Myer YP, Vinogradov SN. Complex formation between methionine and a heme peptide from cytochrome c.. Proc Natl Acad Sci U S A 1965 Dec;54(6):1658-64.
              pmc: PMC300530pubmed: 5218919doi: 10.1073/pnas.54.6.1658google scholar: lookup
            17. Hawkins BK, Hilgenwillis S, Pielak GJ, Dawson JH. Novel axial ligand interchange in Cytochrome c: Incorporation of a histidine at position 82 leads to displacement of the wild-type methionine-80 ligand. J. Am. Chem. Soc. 116: 3111–3112.
            18. Jones CM, Henry ER, Hu Y, Chan CK, Luck SD, Bhuyan A, Roder H, Hofrichter J, Eaton WA. Fast events in protein folding initiated by nanosecond laser photolysis.. Proc Natl Acad Sci U S A 1993 Dec 15;90(24):11860-4.
              pmc: PMC48084pubmed: 8265638doi: 10.1073/pnas.90.24.11860google scholar: lookup
            19. Keilin D. Cytochrome and intracellular oxidase. Proc. R. Soc. Lond. B 106: 418–444.
            20. Keilin D, Hartree EF. Preparation of pure cytochrome c from heart muscle and some of its properties. Proc. R. Soc. Lond. B 122: 298–313.
            21. Knapp JA, Pace CN. Guanidine hydrochloride and acid denaturation of horse, cow, and Candida krusei cytochromes c.. Biochemistry 1974 Mar 12;13(6):1289-94.
              pubmed: 4360785doi: 10.1021/bi00703a036google scholar: lookup
            22. Margalit R, Schejter A. Cytochrome c: a thermodynamic study of the relationships among oxidation state, ion-binding and structural parameters. 1. The effects of temperature, pH and electrostatic media on the standard redox potential of cytochrome c.. Eur J Biochem 1973 Feb 1;32(3):492-9.
              pubmed: 4348126doi: 10.1111/j.1432-1033.1973.tb02633.xgoogle scholar: lookup
            23. Margoliash E, Schejter A. Cytochrome c. Adv. Protein Chem. 21: 126–213.
            24. Margoliash E, Walassek OF. Cytochrome c from vertebrate and invertebrate sources. Methods Enzymol. 10: 339–348.
            25. Ramely L, Kranse Jr MS. Theory of square wave voltammetry. Anal. Chem. 41: 1362–1365.
            26. Rudolph M. An algorithm of general application for the digital simulation of electrochemical processes. J. Electroanal. Chem. 292: 1–7.
            27. Rudolph M. Digital simulations with the fast implicit finite difference algorithm: The development of a general simulator for electrochemical processes. In Physical electrochemistry: Principles, methods, and applications (ed. I. Rubinstein), pp. 81–129.
            28. Rudolph M, Reddy DP, Feldberg SW. A simulator for cyclic voltammetric responses. Anal. Chem. 66: A589–A600.
            29. 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):1552-7.
              pubmed: 5461955
            30. Schejter A, Taler G, Navon G, Liu X-J, Margoliash E. Oxidation state-induced change of iron ligand in the phenylalanine-82 to histidine mutant of yeast iso-1-cytochrome c. J. Am. Chem. Soc. 118: 477–478.
            31. Schejter A, Sanishvili R, Qin W, Margoliash E. A comparison of local and global effects of mutations of mammalian cytochrome c. Chemtracts—Biochem. Mol. Biol. 11: 713–728.
            32. Smith ET, Feinberg BA. Redox properties of several bacterial ferredoxins using square wave voltammetry.. J Biol Chem 1990 Aug 25;265(24):14371-6.
              pubmed: 2387857
            33. Smith ET, Bennett DW, Feinberg BA. Redox properties of 2[4Fe-4S] ferredoxins. Anal. Chim. Acta 251: 27–33.
            34. Takano T, Dickerson RE. 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.
              pubmed: 6279867doi: 10.1016/0022-2836(81)90528-3google scholar: lookup
            35. Taniguchi V, Sailasuta-Scott N, Anson FC, Gray HB. Thermodynamics of metalloprotein electron transfer reactions. Pure Appl. Chem. 52: 2275–2281.
            36. Trewhella J, Carlson VA, Curtis EH, Heidorn DB. Differences in the solution structures of oxidized and reduced cytochrome c measured by small-angle X-ray scattering.. Biochemistry 1988 Feb 23;27(4):1121-5.
              pubmed: 2835084doi: 10.1021/bi00404a007google scholar: lookup

            Citations

            This article has been cited 8 times.
            1. Naiyer A, Khan B, Hussain A, Islam A, Alajmi MF, Hassan MI, Sundd M, Ahmad F. Stability of uniformly labeled ((13)C and (15)N) cytochrome c and its L94G mutant. Sci Rep 2021 Mar 24;11(1):6804.
              doi: 10.1038/s41598-021-86332-wpubmed: 33762670google scholar: lookup
            2. Varghese F, Kabasakal BV, Cotton CAR, Schumacher J, Rutherford AW, Fantuzzi A, Murray JW. A low-potential terminal oxidase associated with the iron-only nitrogenase from the nitrogen-fixing bacterium Azotobacter vinelandii. J Biol Chem 2019 Jun 14;294(24):9367-9376.
              doi: 10.1074/jbc.RA118.007285pubmed: 31043481google scholar: lookup
            3. Salimi A, Motaharitabar E, Goudarzi M, Rezaie A, Kalantari H. Toxicity evaluation of microemulsion (nano size) of sour cherry kernel extract for the oral bioavailability enhancement. Jundishapur J Nat Pharm Prod 2014 Feb;9(1):16-23.
              doi: 10.17795/jjnpp-14370pubmed: 24644434google scholar: lookup
            4. 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
            5. Dai Y, Zheng Y, Swain GM, Proshlyakov DA. Equilibrium and kinetic behavior of Fe(CN)6(3-/4-) and cytochrome c in direct electrochemistry using a film electrode thin-layer transmission cell. Anal Chem 2011 Jan 15;83(2):542-8.
              doi: 10.1021/ac102113vpubmed: 21166441google scholar: lookup
            6. Lin PC, Türk K, Häse CC, Fritz G, Steuber J. Quinone reduction by the Na+-translocating NADH dehydrogenase promotes extracellular superoxide production in Vibrio cholerae. J Bacteriol 2007 May;189(10):3902-8.
              doi: 10.1128/JB.01651-06pubmed: 17322313google scholar: lookup
            7. 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
            8. Chertkova RV, Oleynikov IP, Pakhomov AA, Sudakov RV, Semenova MA, Arutyunyan AM, Ptushenko VV, Kirpichnikov MP, Dolgikh DA, Vygodina TV. The Increase in the Peroxidase Activity of the Cytochrome C with Substitutions in the Universal Binding Site Is Associated with Changes in the Ability to Interact with External Ligands. Int J Mol Sci 2024 Jul 28;25(15).
              doi: 10.3390/ijms25158237pubmed: 39125806google scholar: lookup
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