Detection and interpretation of redox potential optima in the catalytic activity of enzymes

被引:43
作者
Elliott, SJ
Léger, C
Pershad, HR
Hirst, J
Heffron, K
Ginet, N
Blasco, F
Rothery, RA
Weiner, JH
Armstrong, FA
机构
[1] Univ Oxford, Inorgan Chem Lab, Oxford OX1 3QR, England
[2] MRC, Dunn Human Nutr Unit, Cambridge CB2 2XY, England
[3] CNRS, Chim Bacterienne Lab, IBSM, F-13402 Marseille, France
[4] Univ Alberta, Dept Biochem, Edmonton, AB T6G 2H7, Canada
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2002年 / 1555卷 / 1-3期
基金
英国生物技术与生命科学研究理事会;
关键词
oxidoreductase; voltammetry; respiration; electron transport; redox enzyme; electrochemistry;
D O I
10.1016/S0005-2728(02)00254-2
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
It is no surprise that the catalytic activity of electron-transport enzymes may be optimised at certain electrochemical potentials in ways that are analogous to observations of pH-rate optima. This property is observed clearly in experiments in which an enzyme is adsorbed on an electrode surface which can supply or receive electrons rapidly and in a highly controlled manner. In such a way, the rate of catalysis can be measured accurately as a function of the potential (driving force) that is applied. In this paper, we draw attention to a few examples in which this property has been observed in enzymes that are associated with membrane-bound respiratory chains, and we discuss its possible origins and implications for in vivo regulation. (C) 2002 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:54 / 59
页数:6
相关论文
共 18 条
[1]   Progress in understanding structure-function relationships in respiratory chain complex II [J].
Ackrell, BAC .
FEBS LETTERS, 2000, 466 (01) :1-5
[2]   CLASSIFICATION OF FUMARATE REDUCTASES AND SUCCINATE DEHYDROGENASES BASED UPON THEIR CONTRASTING BEHAVIOR IN THE REDUCED BENZYLVIOLOGEN FUMARATE ASSAY [J].
ACKRELL, BAC ;
ARMSTRONG, FA ;
COCHRAN, B ;
SUCHETA, A ;
YU, T .
FEBS LETTERS, 1993, 326 (1-3) :92-94
[3]   Catalytic protein film voltammetry from a respiratory nitrate reductase provides evidence for complex electrochemical modulation of enzyme activity [J].
Anderson, LJ ;
Richardson, DJ ;
Butt, JN .
BIOCHEMISTRY, 2001, 40 (38) :11294-11307
[4]  
[Anonymous], CONT ENZYME KINETICS
[5]   Insights from protein film voltammetry into mechanisms of complex biological electron-transfer reactions [J].
Armstrong, FA .
JOURNAL OF THE CHEMICAL SOCIETY-DALTON TRANSACTIONS, 2002, (05) :661-671
[6]   Reactions of complex metalloproteins studied by protein-film voltammetry [J].
Armstrong, FA ;
Heering, HA ;
Hirst, J .
CHEMICAL SOCIETY REVIEWS, 1997, 26 (03) :169-179
[7]   The coordination and function of the redox centres of the membrane-bound nitrate reductases [J].
Blasco, F ;
Guigliarelli, B ;
Magalon, A ;
Asso, M ;
Giordano, G ;
Rothery, RA .
CELLULAR AND MOLECULAR LIFE SCIENCES, 2001, 58 (02) :179-193
[8]  
Hagerhall C, 1997, BBA-BIOENERGETICS, V1320, P107, DOI 10.1016/S0005-2728(97)00019-4
[9]   Direct detection and measurement of electron relays in a multicentered enzyme: Voltammetry of electrode-surface films of E-coli fumarate reductase, an iron-sulfur flavoprotein [J].
Heering, HA ;
Weiner, JH ;
Armstrong, FA .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1997, 119 (48) :11628-11638
[10]   Determination of an optimal potential window for catalysis by E-coli dimethyl sulfoxide reductase and hypothesis on the role of Mo(V) in the reaction pathway [J].
Heffron, K ;
Léger, C ;
Rothery, RA ;
Weiner, JH ;
Armstrong, FA .
BIOCHEMISTRY, 2001, 40 (10) :3117-3126