Review article: structural and functional properties of cytochrome aa3 from bacteria.

J A García-Horsman, E Escamilla
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Abstract

The aa3 oxidases from bacteria form a group of related enzymes that resemble the far more complex mitochondrial cytochrome c oxidase, both functionally and structurally. These enzymes catalyze electron transfer from ferrocytochrome c to oxygen to produce water. This transfer is coupled to proton translocation. Several oxidases of this type have been purified from cytoplasmic membranes of bacteria. This review summarizes the present knowledge on purified bacterial aa3 oxidases and correlates these findings with data available for the eukaryotic cytochrome c-oxidases.

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综述文章:细菌细胞色素aa3的结构和功能特性。
细菌的aa3氧化酶形成了一组相关的酶,在功能和结构上都类似于复杂得多的线粒体细胞色素c氧化酶。这些酶催化从铁细胞色素c到氧的电子转移以产生水。这种转移与质子易位相结合。这种类型的氧化酶已经从细菌的细胞质膜中纯化出来。本文综述了目前对纯化细菌aa3氧化酶的研究进展,并将这些发现与真核细胞色素c氧化酶的研究结果进行了比较。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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