Coupled proton and electron transfer reactions in cytochrome oxidase

被引:85
作者
Gennis, RB [1 ]
机构
[1] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA
关键词
cytochrome; oxidase; bioenergetics; proton motive force; voltage; channels; protons; reiew;
D O I
10.2741/1237
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
Cytochrome oxidase catalyzes the four-electron reduction of O-2 to water and conserves the substantial free energy of the reaction in the form of a protonmotive force. For each electron, two full charges are translocated across the membrane, resulting in a voltage. One of the mechanisms to generate the charge separation in cytochrome oxidase is via a proton pump. A single reaction cycle can be monitored over the course of about 1 msec using absorption spectroscopy, revealing distinct intermediates. Thus, the reaction cycle can be studied as a series of steps. Each of the reaction steps in the catalytic cycle involves a sequence of coupled electron and proton transfer reaction, where protons are either consumed in the chemistry of water formation or pumped across the membrane. The pumping mechanism requires consideration of both the thermodynamics of the various species but also the favored kinetic pathways that assure proton pumping is unidirectional. Hence, a knowledge of transition states and transiently, poorly populated intermediates is likely to be important to understand the mechanism of the pump.
引用
收藏
页码:581 / 591
页数:11
相关论文
共 75 条
[1]  
Abramson J, 2000, NAT STRUCT BIOL, V7, P910
[2]   Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R-sphaeroides [J].
Adelroth, P ;
Gennis, RB ;
Brzezinski, P .
BIOCHEMISTRY, 1998, 37 (08) :2470-2476
[3]  
ADELROTH P, 1995, BIOCHEMISTRY-US, V34, P2844
[4]   Proton transfer from glutamate 286 determines the transition rates between oxygen intermediates in cytochrome c oxidase [J].
Ådelroth, P ;
Karpefors, M ;
Gilderson, G ;
Tomson, FL ;
Gennis, RB ;
Brzezinski, P .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2000, 1459 (2-3) :533-539
[5]   Hydrogen bonds, water rotation and proton mobility [J].
Agmon, N .
JOURNAL DE CHIMIE PHYSIQUE ET DE PHYSICO-CHIMIE BIOLOGIQUE, 1996, 93 (10) :1714-1736
[6]   THE GROTTHUSS MECHANISM [J].
AGMON, N .
CHEMICAL PHYSICS LETTERS, 1995, 244 (5-6) :456-462
[7]   How oxygen is activated and reduced in respiration [J].
Babcock, GT .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (23) :12971-12973
[8]   Time-resolved step-scan Fourier transform infrared spectroscopy of the CO adducts of bovine cytochrome c oxidase and of cytochrome bo3 from Escherichia coli [J].
Bailey, JA ;
Tomson, FL ;
Mecklenburg, SL ;
MacDonald, GM ;
Katsonouri, A ;
Puustinen, A ;
Gennis, RB ;
Woodruff, WH ;
Dyer, RB .
BIOCHEMISTRY, 2002, 41 (08) :2675-2683
[9]   Redox dependent changes at the heme propionates in cytochrome c oxidase from Paracoccus denitrificans:: Direct evidence from FTIR difference spectroscopy in combination with heme propionate 13C labeling [J].
Behr, J ;
Hellwig, P ;
Mäntele, W ;
Michel, H .
BIOCHEMISTRY, 1998, 37 (20) :7400-7406
[10]  
BRADEN M, 2002, BIOCHEMISTRY-US, V41, P10794