Biodiversity of cytochrome P450 redox systems.

K J McLean, M Sabri, K R Marshall, R J Lawson, D G Lewis, D Clift, P R Balding, A J Dunford, A J Warman, J P McVey, A-M Quinn, M J Sutcliffe, N S Scrutton, A W Munro

Journal: Biochemical Society transactions 2005;33(Pt 4):796-801

PMID: 16042601

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Abstract

P450s (cytochrome P450 mono-oxygenases) are a superfamily of haem-containing mono-oxygenase enzymes that participate in a wide range of biochemical pathways in different organisms from all of the domains of life. To facilitate their activity, P450s require sequential delivery of two electrons passed from one or more redox partner enzymes. Although the P450 enzymes themselves show remarkable similarity in overall structure, it is increasingly apparent that there is enormous diversity in the redox partner systems that drive the P450 enzymes. This paper examines some of the recent advances in our understanding of the biodiversity of the P450 redox apparatus, with a particular emphasis on the redox systems in the pathogen Mycobacterium tuberculosis.

Address: Department of Biochemistry, University of Leicester, The Henry Wellcome Building, Lancaster Road, Leicester LE1 9HN, UK. [email protected]

DOI: 10.1042/BST0330796

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MeSH Terms: Bacterial Proteins, Binding Sites, Biodiversity, Cytochrome P-450 Enzyme System, Electron Transport, Ferredoxins, Flavin-Adenine Dinucleotide, Flavodoxin, Genome, Bacterial, Models, Molecular, Mycobacterium tuberculosis, NADP, Oxidation-Reduction, Protein Conformation