CHARACTERIZATION OF CYTOCHROME C FROM NITROBACTER AGILIS

被引:14
作者
KETCHUM, PA
SANDERS, HK
GRYDER, JW
NASON, A
机构
[1] McCollum-Pratt Institute, the Department of Chemistry, The Johns Hopkins University, Baltimore
基金
美国国家卫生研究院;
关键词
D O I
10.1016/0005-2728(69)90167-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Cytochrome c from Nitrobacter agilis was isolated and purified approx. 60-fold. Absorption spectra of both the oxidized and the reduced Nitrobacter cytochrome c and the oxidized minus reduced difference spectrum of this cytochrome were essentially identical to the corresponding spectra of horse-heart cytochrome c. The redox potential of this cytochrome was determined by spectrophotometric titration with ferrocyanide/ferricyanide and found to be +0.282 V over the pH range 6.0 to 8.7, while a potential of +0.265 V was determined in the same manner for horse-heart cytochrome c. The titration also indicated that the Nitrobacter ferrocytochrome is oxidized by a single electron transfer. © 1969.
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页码:360 / &
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