Biodiversity of cytochrome P450 redox systems. (1st August 2005)

• Record Type: Journal Article
• Authors: McLean, K.J.; Sabri, M.; Marshall, K.R.; Lawson, R.J.; Lewis, D.G.; Clift, D.; Balding, P.R.; Dunford, A.J.; Warman, A.J.; McVey, J.P.; Quinn, A.-M.; Sutcliffe, M.J.; Scrutton, N.S.; Munro, A.W.
• Is Part Of: Biochemical Society transactions. Volume 33:Number 4(2005)
• Page Start: 796
• Page End: 801
• Publication Date: 2005-08-01
• Subjects: biodiversity -- cytochrome P450 -- electron transfer -- ferredoxin -- flavoprotein -- redox partner system; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0330796
• Languages: English
• ISSNs: 0300-5127

Abstract

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 .