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
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
收藏
页码:579 / 591
页数:13
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