STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF CYTOCHROME-C-OXIDASE FROM PARACOCCUS-DENITRIFICANS
STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF CYTOCHROME-C-OXIDASE FROM PARACOCCUS-DENITRIFICANS
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DOI：
10.1038/376660a0
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发表时间：
1995-08-24
期刊：
影响因子：
64.8
通讯作者：
MICHEL, H
中科院分区：
文献类型：
--
作者：
IWATA, S;OSTERMEIER, C;MICHEL, H
本文报道了从土壤细菌Paracoccus denitriicans分离得到的含有细胞色素C氧化酶的四个蛋白质亚基与抗体F-v片段络合的2.8埃分辨率的晶体结构。亚基I包含12个跨膜的，主要是螺旋片段，并结合血红素A和血红素A(3)-铜B双核中心，在那里分子氧被还原为水。可以确定两条质子转移途径，一条用于水形成过程中消耗的质子，另一条用于‘质子抽运’。讨论了质子泵浦的机理。
The crystal structure at 2.8 Angstrom resolution of the four protein subunits containing cytochrome c oxidase from the soil bacterium Paracoccus denitrificans, complexed with an antibody F-v fragment, is described. Subunit I contains 12 membrane-spanning, primarily helical segments and binds haem a and the haem a(3)-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.