Characterization of cytochrome b in the isolated ubiquinol‐cytochrome c 2 oxidoreductase from Rhodopseudomonas sphaeroides GA
Characterization of cytochrome b in the isolated ubiquinol‐cytochrome c
2 oxidoreductase from Rhodopseudomonas sphaeroides GA
复制标题
分离的泛醇细胞色素 c 中细胞色素 b 的表征
DOI:
10.1016/0014-5793(83)80136-7
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发表时间:
1983
期刊:
影响因子:
3.5
通讯作者:
G. Hauska
中科院分区:
文献类型:
--
作者:
N. Gabellini;G. Hauska
Extinction coefficients for cytochromebandc1in the isolated cytochromebc1complex fromRhodopseudomonas sphaeroidesGA have been determined. They are 25 mM−1.cm−1at 561 nm for cytochromeband 17.4 mM−1.cm−1at 553 nM for cytochromec1for the difference between the reduced and the oxidized state. Cytochromebis present in two forms in the complex. One form has anEm7of 50 mV, an α-peak of 557 nm at liquid N2temperature and of 561 nm at RT, which is red-shifted by antimycin A. The other form has anEm7of −90 mV, a double α-peak of 555 and 561 nm at liquid N2temperature corresponding to 559 and 566 nm at RT. The absorption at 566 nm is red-shifted by myxothiazol. The two shifts are independent of each other. Both midpoint potentials of cytochromesbare pH-dependent. The redox center compositions of the cytochromebc1complexes fromRhodopseudomonas sphaeroidesand from mitochondria are identical.