Structure of caa3 cytochrome c oxidase - a nature-made enzyme-substrate complex

被引：10

作者：

Noor, Mohamed Radzi ^{[1
,2
]}

Soulimane, Tewfik ^{[1
,2
]}

机构：

[1] Univ Limerick, Dept Chem & Environm Sci, Limerick, Ireland

[2] Univ Limerick, Mat & Surface Sci Inst MSSI, Limerick, Ireland

来源：

BIOLOGICAL CHEMISTRY | 2013年 / 394卷 / 05期

基金：

爱尔兰科学基金会;

关键词：

ba(3) oxidase; caa(3) oxidase; respiratory complex; subunit IV; terminal oxidase; Thermus thermophilus; SUBUNIT-III; THERMUS-THERMOPHILUS; D-PATHWAY; OXYGEN REDUCTASE; PROTON UPTAKE; NITRIC-OXIDE; PROTEIN; BA(3); LIPIDS; INACTIVATION;

D O I：

10.1515/hsz-2012-0343

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：

Aerobic respiration, the energetically most favorable metabolic reaction, depends on the action of terminal oxidases that include cytochrome c oxidases. The latter forms a part of the heme-copper oxidase superfamily and consists of three different families (A, B, and C types). The crystal structures of all families have now been determined, allowing a detailed structural comparison from evolutionary and functional perspectives. The A2-type oxidase, exemplified by the Thermus thermophilus caa(3) oxidase, contains the substrate cytochrome c covalently bound to the enzyme complex. In this article, we highlight the various features of caa(3) enzyme and provide a discussion of their importance, including the variations in the proton and electron transfer pathways.

引用

页码：579 / 591

页数：13

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