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 N 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 N Daff
, Caroline S Miles
, Stephen K Chapman
, Dominikus A Lysek
, Christopher C Moser
, Christopher C Page
, P Leslie Dutton

Research output: Contribution to journal › Literature review › peer-review

392 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 - May 2002

Keywords

CATALYTIC CYCLE
P-450 BM3
DOMAIN MOVEMENT
BINDING
ELECTRON-TRANSFER
REDUCTASE
PROTEIN
CYTOCHROME P450
BACILLUS-MEGATERIUM
SUBSTRATE

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10.1016/S0968-0004(02)02086-8

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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 = "CATALYTIC CYCLE, P-450 BM3, DOMAIN MOVEMENT, BINDING, ELECTRON-TRANSFER, REDUCTASE, PROTEIN, CYTOCHROME P450, BACILLUS-MEGATERIUM, SUBSTRATE",

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

year = "2002",

month = may,

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

language = "English",

volume = "27",

pages = "250--257",

journal = "Trends in Biochemical Sciences",

issn = "0968-0004",

publisher = "Elsevier Ltd",

number = "5",

}

TY - JOUR

T1 - P450 BM3: 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 N

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

Y1 - 2002/5

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 - CATALYTIC CYCLE

KW - P-450 BM3

KW - DOMAIN MOVEMENT

KW - BINDING

KW - ELECTRON-TRANSFER

KW - REDUCTASE

KW - PROTEIN

KW - CYTOCHROME P450

KW - BACILLUS-MEGATERIUM

KW - SUBSTRATE

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

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

M3 - Literature review

SN - 0968-0004

VL - 27

SP - 250

EP - 257

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

IS - 5

ER -

P450 BM3: the very model of a modern flavocytochrome

Abstract

Keywords

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