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

doi:10.1042/BST0330796

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

University of Leicester

Research output: Contribution to journal › Conference article › peer-review

103 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 language	English
Pages (from-to)	796-801
Number of pages	6
Journal	Biochemical Society Transactions
Volume	33
Issue number	4
DOIs	https://doi.org/10.1042/BST0330796
Publication status	Published - 1 Aug 2005
Externally published	Yes
Event	Coenzymology: the biochemistry of vitamin biogenesis and cofactorcontaining enzymes - Kings College, Cambridge, United Kingdom Duration: 4 Apr 2005 → 7 Apr 2005

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SDG 3 Good Health and Well-being

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title = "Biodiversity of cytochrome P450 redox systems",

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.",

keywords = "Biodiversity, Cytochrome p450, Electron transfer, Ferredoxin, Flavoprotein, Redox partner system",

author = "McLean, \{K. J.\} and M. Sabri and Marshall, \{K. R.\} and Lawson, \{R. J.\} and Lewis, \{D. G.\} and D. Clift and Balding, \{P. R.\} and Dunford, \{A. J.\} and Warman, \{A. J.\} and McVey, \{J. P.\} and Quinn, \{A. M.\} and Sutcliffe, \{M. J.\} and Scrutton, \{N. S.\} and Munro, \{A. W.\}",

year = "2005",

month = aug,

day = "1",

doi = "10.1042/BST0330796",

language = "English",

volume = "33",

pages = "796--801",

journal = "Biochemical Society Transactions",

issn = "0300-5127",

publisher = "Portland Press Ltd.",

number = "4",

note = "Coenzymology : the biochemistry of vitamin biogenesis and cofactorcontaining enzymes ; Conference date: 04-04-2005 Through 07-04-2005",

}

TY - JOUR

T1 - Biodiversity of cytochrome P450 redox systems

AU - McLean, K. J.

AU - Sabri, M.

AU - Marshall, K. R.

AU - Lawson, R. J.

AU - Lewis, D. G.

AU - Clift, D.

AU - Balding, P. R.

AU - Dunford, A. J.

AU - Warman, A. J.

AU - McVey, J. P.

AU - Quinn, A. M.

AU - Sutcliffe, M. J.

AU - Scrutton, N. S.

AU - Munro, A. W.

PY - 2005/8/1

Y1 - 2005/8/1

N2 - 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.

AB - 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.

KW - Biodiversity

KW - Cytochrome p450

KW - Electron transfer

KW - Ferredoxin

KW - Flavoprotein

KW - Redox partner system

UR - https://www.scopus.com/pages/publications/23844442197

U2 - 10.1042/BST0330796

DO - 10.1042/BST0330796

M3 - Conference article

C2 - 16042601

AN - SCOPUS:23844442197

SN - 0300-5127

VL - 33

SP - 796

EP - 801

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

IS - 4

T2 - Coenzymology

Y2 - 4 April 2005 through 7 April 2005

ER -

Biodiversity of cytochrome P450 redox systems

Abstract

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