The Rhodospirillum rubrum cytochrome bc1 complex: peptide composition, prosthetic group content and quinone binding.
The Rhodospirillum rubrum cytochrome bc1 complex: peptide composition, prosthetic group content and quinone binding.
复制标题
红色红螺菌细胞色素 bc1 复合物:肽组成、辅基含量和醌结合。
DOI:
10.1016/s0005-2728(89)80190-2
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发表时间:
1989
期刊:
影响因子:
--
通讯作者:
Knaff,DB
中科院分区:
文献类型:
--
作者:
Kriauciunas,A;Yu,L;Yu,CA;Wynn,RM;Knaff,DB
A cytochromebc1complex, essentially free of bacteriochlorophyll, has been purified from the photosynthetic purple non-sulfur bacteriumRhodospirillum rubrum. The complex catalyzes electron flow from quinol to cytochromec(turnover number = 75s−1)that is inhibited by low concentrations of antimycin A and myxothiazol. The complex contains only three peptide subunits: cytochromeb(Mr= 35000); cytochromec1(Mr= 31000) and the Rieske iron-sulfur protein (Mr= 22400).Emvalues (pH 7.4) were measured for cytochrome c, (+ 320 mV) and the two hemes of cytochromeb(− 33 and −90 mV). Electron flow from quinol to cytochromecis inhibited when the complex is pre-illuminated in the presence of a ubiquinone photoaffinity analog (azido-Q). During illumination, the azido-Q becomes covalently attached to the cytochromebpeptide and, to a lesser extent, to cytochromec1.