Evolution of bioinorganic motifs in P450-containing systems.
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.
Degtyarenko
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KN
EMBL Outstation, European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, U.K. kirill@ebi.ac.uk
Kulikova
T A
TA
D020816:Amino Acid Motifs; D001665:Binding Sites; D003067:Coenzymes / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000378:metabolism*; D015786:Cytochromes b5 / Q000378:metabolism; D019143:Evolution, Molecular; D005287:Ferredoxin-NADP Reductase / Q000737:chemistry / Q000378:metabolism; D005288:Ferredoxins / Q000378:metabolism; D046911:Macromolecular Substances; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry / Q000378:metabolism; D009251:NADPH-Ferrihemoprotein Reductase / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary
D003067:Coenzymes; D005288:Ferredoxins; D046911:Macromolecular Substances; D015786:Cytochromes b5; D003577:Cytochrome P-450 Enzyme System; D005287:Ferredoxin-NADP Reductase; D009247:NADH, NADPH Oxidoreductases; D009251:NADPH-Ferrihemoprotein Reductase; C022486:putidaredoxin reductase