Ludwig B, Suda K, Cerletti N
Eur J Biochem. 1983 Dec 15;137(3):597-602. doi: 10.1111/j.1432-1033.1983.tb07867.x.
Cytochrome c1 was purified from the bacterium Paracoccus denitrificans. It is an acidic, hydrophobic polypeptide with an apparent molecular weight of around 65000 and a single, covalently attached heme; it cross-reacts immunologically with cytochrome c1 from yeast mitochondria. The amino acid sequence of the tryptic heme peptide of the bacterial cytochrome c1 shows extensive homology to the corresponding region of beef heart cytochrome c1 [Wakabayashi, S. et al. (1982) J. Biol. Chem. 257, 9335-9344]. Positive evidence for a stable association of the Paracoccus cytochrome c1 with other polypeptides and b-type heme components ('bc1-complex') has not yet been obtained.
细胞色素c1是从反硝化副球菌中纯化得到的。它是一种酸性疏水多肽,表观分子量约为65000,含有一个共价连接的血红素;它与酵母线粒体中的细胞色素c1发生免疫交叉反应。细菌细胞色素c1的胰蛋白酶血红素肽的氨基酸序列与牛心细胞色素c1的相应区域具有广泛的同源性[Wakabayashi, S.等人(1982)《生物化学杂志》257, 9335 - 9344]。尚未获得反硝化副球菌细胞色素c1与其他多肽和b型血红素成分(“bc1复合体”)稳定结合的阳性证据。