P450BM3: the very model of a modern flavocytochrome

A W  Munro; D G  Leys; K J  McLean; K R  Marshall; T W B  Ost; S  Daff; C S  Miles; S K  Chapman; D A  Lysek; C C  Moser; C C  Page; P L  Dutton

P450BM3: the very model of a modern flavocytochrome

A W Munro
, D G Leys
, K J McLean
, K R Marshall
, T W B Ost
, S Daff
, C S Miles
, S K Chapman
, D A Lysek
, C C Moser
, C C Page
, P L Dutton

School of Chemistry

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

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
Publication status	Published - May 2002

Keywords / Materials (for Non-textual outputs)

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

Cite this

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title = "P450BM3: 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 = "ELECTRON-TRANSFER, BACILLUS-MEGATERIUM, CYTOCHROME P450, CATALYTIC CYCLE, DOMAIN MOVEMENT, P-450 BM3, SUBSTRATE, BINDING, REDUCTASE, PROTEIN",

author = "Munro, \{A W\} and Leys, \{D G\} and McLean, \{K J\} and Marshall, \{K R\} and Ost, \{T W B\} and S Daff and Miles, \{C S\} and Chapman, \{S K\} and Lysek, \{D A\} and Moser, \{C C\} and Page, \{C C\} and Dutton, \{P L\}",

year = "2002",

month = may,

language = "English",

volume = "27",

pages = "250--257",

journal = "Trends in biochemical sciences",

issn = "0968-0004",

publisher = "Elsevier",

number = "5",

}

TY - JOUR

T1 - P450BM3: the very model of a modern flavocytochrome

AU - Munro, A W

AU - Leys, D G

AU - McLean, K J

AU - Marshall, K R

AU - Ost, T W B

AU - Daff, S

AU - Miles, C S

AU - Chapman, S K

AU - Lysek, D A

AU - Moser, C C

AU - Page, C C

AU - Dutton, P L

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 - ELECTRON-TRANSFER

KW - BACILLUS-MEGATERIUM

KW - CYTOCHROME P450

KW - CATALYTIC CYCLE

KW - DOMAIN MOVEMENT

KW - P-450 BM3

KW - SUBSTRATE

KW - BINDING

KW - REDUCTASE

KW - PROTEIN

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 -

P450BM3: the very model of a modern flavocytochrome

Abstract

Keywords / Materials (for Non-textual outputs)

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