Gabellini N, Bowyer J R, Hurt E, Melandri B A, Hauska G
Eur J Biochem. 1982 Aug;126(1):105-11. doi: 10.1111/j.1432-1033.1982.tb06753.x.
A cytochrome b/c1 complex which catalyses the reduction of cytochrome c by ubiquinol has been isolated from Rhodopseudomonas sphaeroides GA. It contains two hemes b and substoichiometric amounts of ubiquinone-10 and of the Rieske Fe-S center per cytochrome c1, and is essentially free of reaction center and bacteriochlorophyll. The complex consists of three major polypeptides with apparent molecular masses of 40, 34 and 25 kDa. The 34-kDa polypeptide carries heme. Cytochrome c1 has a midpoint potential of 285 mV. For cytochrome b two midpoint potentials, at 50 and -60 mV, at pH 7.4, can be derived if one assumes two components of equal amount. Ubiquinol--cytochrome c oxidoreductase activity is specific for ubiquinol and bacterial cytochromes c, and is inhibited by antimycin A and 5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole. The complex shows oxidant-induced reduction of cytochrome b.
已从球形红假单胞菌GA中分离出一种细胞色素b/c1复合物，它催化泛醇将细胞色素c还原。每个细胞色素c1含有两个血红素b以及化学计量不足的泛醌-10和 Rieske铁硫中心，并且基本上不含反应中心和细菌叶绿素。该复合物由三种主要多肽组成，其表观分子量分别为40、34和25 kDa。34 kDa的多肽携带血红素。细胞色素c1的中点电位为285 mV。对于细胞色素b，如果假设两个等量的组分，则在pH 7.4时可得出两个中点电位，分别为50和 -60 mV。泛醇 - 细胞色素c氧化还原酶活性对泛醇和细菌细胞色素c具有特异性，并被抗霉素A和5 - n - 十一烷基 - 6 - 羟基 - 4,7 - 二氧苯并噻唑抑制。该复合物显示出氧化剂诱导的细胞色素b还原。
