{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,30]],"date-time":"2026-06-30T23:51:46Z","timestamp":1782863506760,"version":"3.54.5"},"reference-count":36,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2009,1,1]],"date-time":"2009-01-01T00:00:00Z","timestamp":1230768000000},"content-version":"vor","delay-in-days":1065,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2006,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Contrary to most heme proteins, ferrous cytochrome <jats:italic>c<\/jats:italic> does not bind ligands such as cyanide and CO. In order to quantify this observation, the redox potential of the ferric\/ferrous cytochrome <jats:italic>c<\/jats:italic>\u2013cyanide redox couple was determined for the first time by cyclic voltammetry. Its E<jats:sup>0<\/jats:sup>\u2032 was \u2212240 mV versus SHE, equivalent to \u221223.2 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 <jats:italic>c<\/jats:italic> cyanide complex E<jats:sup>0<\/jats:sup>\u2032, the binding constant of cyanide to the reduced protein was estimated to be 4.7 \u00d7 10<jats:sup>\u22123<\/jats:sup> LM<jats:sup>\u22121<\/jats:sup> 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 <jats:italic>c<\/jats:italic>. For coordination of cyanide to ferrocytochrome <jats:italic>c<\/jats:italic>, the entropy change was earlier experimentally evaluated as 92.4 Jmol<jats:sup>\u22121<\/jats:sup>K<jats:sup>\u22121<\/jats:sup> (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 <jats:italic>c<\/jats:italic> 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.<\/jats:p>","DOI":"10.1110\/ps.051825906","type":"journal-article","created":{"date-parts":[[2006,1,25]],"date-time":"2006-01-25T00:45:39Z","timestamp":1138149939000},"page":"234-241","source":"Crossref","is-referenced-by-count":22,"title":["The redox couple of the cytochrome <i>c<\/i> cyanide complex: The contribution of heme iron ligation to the structural stability, chemical reactivity, and physiological behavior of horse cytochrome <i>c<\/i>"],"prefix":"10.1002","volume":"15","author":[{"given":"Abel","family":"Schejter","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael D.","family":"Ryan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erica R.","family":"Blizzard","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chongyao","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emanuel","family":"Margoliash","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Benjamin A.","family":"Feinberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,1]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-0728(93)80142-5"},{"key":"e_1_2_7_3_1","volume-title":"Electrochemical methods: Fundamentals and applications","author":"Bard A.J.","year":"2001"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00035a012"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(78)53021-8"},{"key":"e_1_2_7_6_1","first-page":"103","volume-title":"Cytochrome c\u2014A multidisciplinary approach","author":"Brayer G.D.","year":"1996"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1098\/rspb.1962.0049"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja00111a001"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.79.3.815"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1021\/cr00103a004"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi981037n"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)44026-X"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.44.10.1013"},{"key":"e_1_2_7_14_1","doi-asserted-by":"crossref","first-page":"1504","DOI":"10.1016\/S0021-9258(18)91343-8","article-title":"The reactivity of ferrocytochrome c with iron\u2010binding ligands","volume":"239","author":"George P.","year":"1964","journal-title":"J. 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