Richter O M, Tao J S, Turba A, Ludwig B
Department of Molecular Genetics, University of Frankfurt, Federal Republic of Germany.
J Biol Chem. 1994 Sep 16;269(37):23079-86.
A quinol oxidase has been purified from the cytoplasmic membrane of Paracoccus denitrificans; its heme composition and CO binding properties identify it as a cytochrome ba3. On SDS gels, the purified enzyme complex is separated into five polypeptides. Using partial peptide sequence information for subunit II, the gene locus has been cloned and sequenced. In a typical operon pattern, four genes were identified: qoxA, -B, -C, and -D, coding for subunits II, I, III, and IV. DNA-derived amino acid sequence comparisons reveal extensive similarities to other members of the terminal oxidase superfamily.
已从反硝化副球菌的细胞质膜中纯化出一种喹啉氧化酶;其血红素组成和一氧化碳结合特性表明它是一种细胞色素ba3。在SDS凝胶上,纯化的酶复合物被分离成五条多肽链。利用亚基II的部分肽序列信息,已克隆并测序了该基因位点。按照典型的操纵子模式,鉴定出四个基因:qoxA、-B、-C和-D,它们分别编码亚基II、I、III和IV。DNA推导的氨基酸序列比较显示,它与末端氧化酶超家族的其他成员有广泛的相似性。