Multiple roles of cysteine in biocatalysis

被引:179
作者
Giles, NM [1 ]
Giles, GI [1 ]
Jacob, C [1 ]
机构
[1] Univ Exeter, Sch Chem, Exeter EX4 4QD, Devon, England
基金
英国惠康基金;
关键词
cysteine; sulfur redox-chemistry; hydrolysis; metal-binding;
D O I
10.1016/S0006-291X(02)02770-5
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
In biology, sulfur frequently occurs in the form of cysteine, an amino acid that fulfills a wide range of different functions in proteins including disulfide formation, metal-binding, electron donation, hydrolysis, and redox-catalysis. The 'redox-chameleon' sulfur appears in several oxidation states in vitro. each of them exhibiting specific reactivity, redox-activity, and metal-binding properties. While cysteine-peptidases rely on reduced cysteine to catalyze hydrolytic reactions, many redox-enzymes use distinctively different cysteine redox-couples for exchange. electron, atom, and radical transfer reactions, Although cysteine and cystine can still be considered as the most abundant forms of cysteine in vivo, other modifications such as cysteine acids and sulfur-centered radicals are becoming increasingly important in biochemical research. As such, the biochemistry of sulfur remains a source of continuous investigation and excitement. (C) 2002 Elsevier Science (USA). All rights reserved.
引用
收藏
页码:1 / 4
页数:4
相关论文
共 16 条
[1]   Physiological functions of thioredoxin and thioredoxin reductase [J].
Arnér, ESJ ;
Holmgren, A .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2000, 267 (20) :6102-6109
[2]  
Brocklehurst K., 1998, COMPREHENSIVE BIOL C, P381
[3]  
Claiborne A, 2001, ADV PROTEIN CHEM, V58, P215
[4]   Radical mechanisms of enzymatic catalysis [J].
Frey, PA .
ANNUAL REVIEW OF BIOCHEMISTRY, 2001, 70 :121-148
[5]   Hypothesis: The role of reactive sulfur species in oxidative stress [J].
Giles, GI ;
Tasker, KM ;
Jacob, C .
FREE RADICAL BIOLOGY AND MEDICINE, 2001, 31 (10) :1279-1283
[6]   Reactive sulfur species: An emerging concept in oxidative stress [J].
Giles, GI ;
Jacob, C .
BIOLOGICAL CHEMISTRY, 2002, 383 (3-4) :375-388
[7]  
HILL J, 1975, J BIOL CHEM, V250, P1734
[8]   THIOREDOXIN [J].
HOLMGREN, A .
ANNUAL REVIEW OF BIOCHEMISTRY, 1985, 54 :237-271
[9]   Inhibitory sites in enzymes: Zinc removal and reactivation by thionein [J].
Maret, W ;
Jacob, C ;
Vallee, BL ;
Fischer, EH .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (05) :1936-1940
[10]   AN L40C MUTATION CONVERTS THE CYSTEINE SULFENIC ACID REDOX CENTER IN ENTEROCOCCAL NADH PEROXIDASE TO A DISULFIDE [J].
MILLER, H ;
MANDE, SS ;
PARSONAGE, D ;
SARFATY, SH ;
HOL, WGJ ;
CLAIBORNE, A .
BIOCHEMISTRY, 1995, 34 (15) :5180-5190