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Cytochrome

Cytochrome c with heme c.

Cytochromes are redox-active proteins containing a heme, with a central iron (Fe) atom at its core, as a cofactor. They are involved in the electron transport chain and redox catalysis. They are classified according to the type of heme and its mode of binding. Four varieties are recognized by the International Union of Biochemistry and Molecular Biology (IUBMB), cytochromes a, cytochromes b, cytochromes c and cytochrome d.[1]

Cytochrome function is linked to the reversible redox change from ferrous (Fe(II)) to the ferric (Fe(III)) oxidation state of the iron found in the heme core.[2] In addition to the classification by the IUBMB into four cytochrome classes, several additional classifications such as cytochrome o[3] and cytochrome P450 can be found in biochemical literature.

  1. ^ "Nomenclature Committee of the International Union of Biochemistry (NC-IUB). Nomenclature of electron-transfer proteins. Recommendations 1989". Journal of Biological Chemistry. 267 (1): 665–677. 1992-01-05. doi:10.1016/S0021-9258(18)48544-4. ISSN 0021-9258. PMID 1309757.
  2. ^ L., Lehninger, Albert (2000). Lehninger Principles of Biochemistry (3rd ed.). New York: Worth Publishers. ISBN 978-1572591530. OCLC 42619569.{{cite book}}: CS1 maint: multiple names: authors list (link)
  3. ^ Puustinen, A.; Wikström, M. (1991-07-15). "The heme groups of cytochrome o from Escherichia coli". Proceedings of the National Academy of Sciences. 88 (14): 6122–6126. Bibcode:1991PNAS...88.6122P. doi:10.1073/pnas.88.14.6122. ISSN 0027-8424. PMC 52034. PMID 2068092.

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