期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 281, 期 41, 页码 30319-30325出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M605955200
关键词
-
资金
- NHLBI NIH HHS [R01 HL016101] Funding Source: Medline
- NIGMS NIH HHS [GM55807] Funding Source: Medline
The spectral and kinetic characteristics of two oxidized states of bovine heart cytochrome c oxidase (CcO) have been compared. The first is the oxidized state of enzyme isolated in the fast form (O) and the second is the form that is obtained immediately after oxidation of fully reduced CcO with O-2 (O-H). No observable differences were found between O and O-H states in: (i) the rate of anaerobic reduction of heme a(3) for both the detergent-solubilized enzyme and for enzyme embedded in its natural membraneous environment, (ii) the one-electron distribution between heme a(3) and Cu-B in the course of the full anaerobic reduction, (iii) the optical and (iv) EPR spectra. Within experimental error of these characteristics both forms are identical. Based on these observations it is concluded that the reduction potentials and the ligation states of heme a(3) and Cu-B are the same for CcO in the O and O-H states.
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