期刊
BIOCHEMICAL SOCIETY TRANSACTIONS
卷 30, 期 -, 页码 653-658出版社
PORTLAND PRESS LTD
DOI: 10.1042/bst0300653
关键词
cytochrome oxidase; Pseudomonas; respiration; spectroscopy
Cytochrome cbb(3) oxidase is a member of the haem-copper oxidase superfamily. It is characterized by its high oxygen affinity, while retaining the ability to pump protons. These attributes are central to its proposed role in bacterial microaerobic metabolism. Recent spectroscopic characterization of both the cytochrome cbb(3) oxidase complex from Pseudomonas stutzeri and the di-haem ccoP subunit expressed separately in Escherichia coli has revealed the presence of a low-spin His/His co-ordinated c-type cytochrome. The low midpoint reduction potential of this haem (E-m < + 100 mV), together with its unexpected ability to bind CO in the reduced state at the expense of the distal histidine ligand, raises questions about the role of the ccoP subunit in the deliver-v of electrons to the active site.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据