Biodiversity of cytochrome P450 redox systems

被引：80

作者：

McLean, KJ ^{[1
]}

Sabri, M ^{[1
]}

Marshall, KR ^{[1
]}

Lawson, RJ ^{[1
]}

Lewis, DG ^{[1
]}

Clift, D ^{[1
]}

Balding, PR ^{[1
]}

Dunford, AJ ^{[1
]}

Warman, AJ ^{[1
]}

McVey, JP ^{[1
]}

Quinn, AM ^{[1
]}

Sutcliffe, MJ ^{[1
]}

Scrutton, NS ^{[1
]}

Munro, AW ^{[1
]}

机构：

[1] Univ Leicester, Dept Biochem, Leicester LE1 9HN, Leics, England

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 2005年 / 33卷

基金：

英国生物技术与生命科学研究理事会;

关键词：

biodiversity; cytochrome P450; electron transfer; ferredoxin; flavoprotein; redox partner system;

D O I：

10.1042/BST0330796

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：796 / 801

页数：6

共 62 条

[1] Ligand probes for heme proteins [J].

Anderson, JLR ;

Chapman, SK .

DALTON TRANSACTIONS, 2005, (01) :13-24

[2]

[Anonymous], 2005, Cytochrome P450: structure, mechanism, and biochemistry, DOI DOI 10.1007/0-387-27447-2_1

[3]

ATKINS WM, 1988, J BIOL CHEM, V263, P18842

[4] Characterization and catalytic properties of the sterol 14α-demethylase from Mycobacterium tuberculosis [J].

Bellamine, A ;

Mangla, AT ;

Nes, WD ;

Waterman, MR .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (16) :8937-8942

[5] A covalent modification of NADP+ revealed by the atomic resolution structure of FprA, a Mycobacterium tuberculosis oxidoreductase [J].

Bossi, RT ;

Aliverti, A ;

Raimondi, D ;

Fischer, F ;

Zanetti, G ;

Ferrari, D ;

Tahallah, N ;

Maier, CS ;

Heck, AJR ;

Rizzi, M ;

Mattevi, A .

BIOCHEMISTRY, 2002, 41 (28) :8807-8818

[6]

BREWER CB, 1988, J BIOL CHEM, V263, P791

[7] PHTHALATE DIOXYGENASE REDUCTASE - A MODULAR STRUCTURE FOR ELECTRON-TRANSFER FROM PYRIDINE-NUCLEOTIDES TO [2FE-2S] [J].

CORRELL, CC ;

BATIE, CJ ;

BALLOU, DP ;

LUDWIG, ML .

SCIENCE, 1992, 258 (5088) :1604-1610

[8] Carbon-carbon bond cleavage by cytochrome P450BioI (CYP107H1) [J].

Cryle, MJ ;

De Voss, JJ .

CHEMICAL COMMUNICATIONS, 2004, (01) :86-87

[9] Redox control of the catalytic cycle of flavocytochrome P-450 BM3 [J].

Daff, SN ;

Chapman, SK ;

Turner, KL ;

Holt, RA ;

Govindaraj, S ;

Poulos, TL ;

Munro, AW .

BIOCHEMISTRY, 1997, 36 (45) :13816-13823

[10] A novel class of self-sufficient cytochrome P450 monooxygenases in prokaryotes [J].

De Mot, R ;

Parret, AHA .

TRENDS IN MICROBIOLOGY, 2002, 10 (11) :502-508

← 1 2 3 4 5 6 7 →