Evolution of bioinorganic motifs in P450-containing systems.

K N Degtyarenko, T A Kulikova

Journal: Biochemical Society transactions 2001;29(Pt 2):139-47

PMID: 11356142

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Abstract

The choice of bioinorganic motifs by Nature results in a spectacular variety of active-site structures even within the same protein family. Here, we use the concept of the bioinorganic motif to discuss the function and evolution of P450-containing and other related systems. Apart from P450, these systems include a FAD flavoprotein or domain, a FMN domain, ferredoxins and cytochrome b(5). Analysis of available complete genomes can shed light on what an ancestral P450-containing system could be.

Address: EMBL Outstation, European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, U.K. [email protected]

DOI: 10.1042/0300-5127:0290139

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MeSH Terms: Amino Acid Motifs, Binding Sites, Coenzymes, Cytochrome P-450 Enzyme System, Cytochromes b5, Evolution, Molecular, Ferredoxin-NADP Reductase, Ferredoxins, Macromolecular Substances, NADH, NADPH Oxidoreductases, NADPH-Ferrihemoprotein Reductase, Protein Structure, Tertiary