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

Research output: Contribution to journalConference article

81 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)796-801
Number of pages6
JournalBiochemical Society Transactions
Volume33
Issue number4
DOIs
Publication statusPublished - 1 Aug 2005
Externally publishedYes
EventCoenzymology: the biochemistry of vitamin biogenesis and cofactorcontaining enzymes - Kings College, Cambridge, United Kingdom
Duration: 4 Apr 20057 Apr 2005

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