P450 BM3: The very model of a modern flavocytochrome

Andrew W. Munro; David G. Leys; Kirsty J. McLean; Ker R. Marshall; Tobias W.B. Ost; Simon Daff; Caroline S. Miles; Stephen K. Chapman; Dominikus A. Lysek; Christopher C. Moser; Christopher C. Page; P. Leslie Dutton

doi:10.1016/S0968-0004(02)02086-8

P450 BM3: The very model of a modern flavocytochrome

Andrew W. Munro, David G. Leys, Kirsty J. McLean, Ker R. Marshall, Tobias W.B. Ost, Simon Daff, Caroline S. Miles, Stephen K. Chapman, Dominikus A. Lysek, Christopher C. Moser, Christopher C. Page, P. Leslie Dutton

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

379 Citations (Scopus)

Abstract

Flavocytochrome P450 BM3 is a bacterial P450 system in which a fatty acid hydroxylase P450 is fused to a mammalian-like diflavin NADPH-P450 reductase in a single polypeptide. The enzyme is soluble (unlike mammalian P450 redox systems) and its fusion arrangement affords it the highest catalytic activity of any P450 mono-oxygenase. This article discusses the fundamental properties of P450 BM3 and how progress with this model P450 has affected our comprehension of P450 systems in general.

Original language	English
Pages (from-to)	250-257
Number of pages	8
Journal	Trends in Biochemical Sciences
Volume	27
Issue number	5
DOIs	https://doi.org/10.1016/S0968-0004(02)02086-8
Publication status	Published - 1 May 2002
Externally published	Yes

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title = "P450 BM3: The very model of a modern flavocytochrome",

abstract = "Flavocytochrome P450 BM3 is a bacterial P450 system in which a fatty acid hydroxylase P450 is fused to a mammalian-like diflavin NADPH-P450 reductase in a single polypeptide. The enzyme is soluble (unlike mammalian P450 redox systems) and its fusion arrangement affords it the highest catalytic activity of any P450 mono-oxygenase. This article discusses the fundamental properties of P450 BM3 and how progress with this model P450 has affected our comprehension of P450 systems in general.",

keywords = "P450 BM3, flavocytochrome, P450 redox systems, Biochemistry, Structural biology",

author = "Munro, {Andrew W.} and Leys, {David G.} and McLean, {Kirsty J.} and Marshall, {Ker R.} and Ost, {Tobias W.B.} and Simon Daff and Miles, {Caroline S.} and Chapman, {Stephen K.} and Lysek, {Dominikus A.} and Moser, {Christopher C.} and Page, {Christopher C.} and Dutton, {P. Leslie}",

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doi = "10.1016/S0968-0004(02)02086-8",

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T2 - The very model of a modern flavocytochrome

AU - Munro, Andrew W.

AU - Leys, David G.

AU - McLean, Kirsty J.

AU - Marshall, Ker R.

AU - Ost, Tobias W.B.

AU - Daff, Simon

AU - Miles, Caroline S.

AU - Chapman, Stephen K.

AU - Lysek, Dominikus A.

AU - Moser, Christopher C.

AU - Page, Christopher C.

AU - Dutton, P. Leslie

PY - 2002/5/1

Y1 - 2002/5/1

N2 - Flavocytochrome P450 BM3 is a bacterial P450 system in which a fatty acid hydroxylase P450 is fused to a mammalian-like diflavin NADPH-P450 reductase in a single polypeptide. The enzyme is soluble (unlike mammalian P450 redox systems) and its fusion arrangement affords it the highest catalytic activity of any P450 mono-oxygenase. This article discusses the fundamental properties of P450 BM3 and how progress with this model P450 has affected our comprehension of P450 systems in general.

AB - Flavocytochrome P450 BM3 is a bacterial P450 system in which a fatty acid hydroxylase P450 is fused to a mammalian-like diflavin NADPH-P450 reductase in a single polypeptide. The enzyme is soluble (unlike mammalian P450 redox systems) and its fusion arrangement affords it the highest catalytic activity of any P450 mono-oxygenase. This article discusses the fundamental properties of P450 BM3 and how progress with this model P450 has affected our comprehension of P450 systems in general.

KW - P450 BM3

KW - flavocytochrome

KW - P450 redox systems

KW - Biochemistry

KW - Structural biology

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U2 - 10.1016/S0968-0004(02)02086-8

DO - 10.1016/S0968-0004(02)02086-8

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AN - SCOPUS:0036558027

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EP - 257

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

SN - 0376-5067

IS - 5

ER -

P450 BM3: The very model of a modern flavocytochrome

Abstract

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