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Biodiversity of cytochrome P450 redox systems

Biochemical Society Transactions
Portland Press
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  • Biology
  • Chemistry
  • Ecology
  • Medicine


bst081.dvi 796 Biochemical Society Transactions (2005) Volume 33, part 4 Biodiversity of cytochrome P450 redox systems K.J. McLean1, 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 and A.W. Munro1 Department of Biochemistry, University of Leicester, The Henry Wellcome Building, Lancaster Road, Leicester LE1 9HN, U.K. 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. Introduction P450s (cytochrome P450 mono-oxygenases) are an ever- growing family of enzymes that show extraordinary diversity in their reaction chemistry [1]. P450s are typically thought of as mono-oxygenases, i.e. catalysing a reductive scission of the dioxygen bound to the haem iron at the core of the P450, leading to the introduction of a single atom from oxygen into an organic substrate and the production of a molecule of water, according to the following equation: RH + O2 + 2e− + 2H+ → ROH + H2O (1) In this equation, RH is the substrate, and protons are de- livered to the catalytic centre of the P450 through active-site amino acid side chains. The proton relay mechanism is critical for the productive cleavage of the O–O bond, and structural and mechanistic studies have implicated a number of amino acids with a

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