ELECTRON-TRANSFER AND LIGAND-BINDING IN TERMINAL OXIDASES - IMPACT OF RECENT STRUCTURAL INFORMATION

被引：14

作者：

BRUNORI, M

ANTONINI, G

GIUFFRE, A

MALATESTA, F

NICOLETTI, F

SARTI, P

WILSON, MT

机构：

[1] UNIV ROMA TOR VERGATA,ROME,ITALY

[2] CNR,CTR MOLEC BIOL,ROME,ITALY

[3] UNIV CAGLIARI,INST BIOL CHEM,CAGLIARI,ITALY

[4] UNIV ESSEX,DEPT CHEM & BIOL CHEM,COLCHESTER CO4 3SQ,ESSEX,ENGLAND

来源：

FEBS LETTERS | 1994年 / 350卷 / 2-3期

关键词：

TERMINAL OXIDASE; STRUCTURAL CHANGE; KINETICS; ELECTRON TRANSFER; METALLOPROTEIN;

D O I：

10.1016/0014-5793(94)00779-9

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：

A consensus structure for the active site of terminal oxidases has been recently proposed by Hosler et al. [(1993) J. Bioenerg. Biomem. 25, 121-135]. We exploit the novel structural information to propose a hypothesis for the large difference in the rate of internal electron transfer found when experiments are started either with the reduced or with the oxidized enzyme. This rationale also allows us to discuss the oxidation state of the prevailing oxygen reacting species with reference to the concentration of the two substrates (oxygen and cytochrome c) and to the structural state of the oxidase.

引用

页码：164 / 168

页数：5

共 30 条

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