Abstract
The evolution of cytochromes P450 has been thoroughly discussed in a number of reviews (Nebert and Gonzalez 1987; Nelson and Strobel 1987; Gonzalez and Nebert 1990). All cytochrome P450 proteins possess a non-covalently bound heme (protoporphyrin IX) and segment of 26 amino acids surrounding a cysteine that is highly conserved. This cysteine donates the thiolate fifth ligand to the heme iron. The amino acid environment surrounding the heme results in a typical cytochrome P450 Soret absorption band at around 450 nm when the iron is reduced by electrons and complexed with carbon monoxide. Any enzyme having these properties would be a “card-holding” member of the cytochrome P450 superfamily.
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Gonzalez, F.J. (1993). Cytochrome P450 Evolution and Nomenclature. In: Schenkman, J.B., Greim, H. (eds) Cytochrome P450. Handbook of Experimental Pharmacology, vol 105. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-77763-9_14
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DOI: https://doi.org/10.1007/978-3-642-77763-9_14
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