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脱氮副球菌细胞色素c氧化酶2.8埃分辨率的结构

Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans.

作者信息

Iwata S, Ostermeier C, Ludwig B, Michel H

机构信息

Max-Planck-Institut für Biophysik, Frankfurt/M., Germany.

出版信息

Nature. 1995 Aug 24;376(6542):660-9. doi: 10.1038/376660a0.

DOI:10.1038/376660a0
PMID:7651515
Abstract

The crystal structure at 2.8 A resolution of the four protein subunits containing cytochrome c oxidase from the soil bacterium Paracoccus denitrificans, complexed with antibody Fv fragment, is described. Subunit I contains 12 membrane-spanning, primarily helical segments and binds haem a and the haem a3-copper B binuclear centre where molecular oxygen is reduced to water. Two proton transfer pathways, one for protons consumed in water formation and one for 'proton pumping', could be identified. Mechanisms for proton pumping are discussed.

摘要

描述了来自反硝化副球菌的含细胞色素c氧化酶的四个蛋白质亚基与抗体Fv片段复合后的2.8埃分辨率晶体结构。亚基I包含12个跨膜的主要为螺旋状的片段,并结合血红素a以及血红素a3-铜B双核中心,在此分子氧被还原为水。可以识别出两条质子转移途径,一条用于水形成过程中消耗的质子,另一条用于“质子泵浦”。讨论了质子泵浦的机制。

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