Buse G, Hensel S, Fee J A
Institut für Biochemie, Rheinisch-Westfälische Technische Hochschule Aachen, Federal Republic of Germany.
Eur J Biochem. 1989 Apr 15;181(1):261-8. doi: 10.1111/j.1432-1033.1989.tb14720.x.
The terminal cytochrome c1aa3 of the respiratory chain of Thermus thermophilus has been isolated and purified to homogeneity by a novel procedure. The two subunit proteins (55 and 33 kDa) have been characterized chemically. Computer searches with partial amino acid sequences obtained from both subunits show that the larger subunit belongs to the cytochrome oxidase subunit I protein family while the smaller covalently heme-binding subunit is not a cytochrome c1 but appears to be a fused protein between cytochrome c and cytochrome oxidase subunit II. With respect to the 16-S rRNA-derived phylogeny of procaryotes, the results show that the genetic information for an O2-reacting cytochrome oxidase (EC 1.9.3.1) existed already in early eubacteria.
嗜热栖热菌呼吸链的末端细胞色素c1aa3已通过一种新方法分离纯化至同质。对这两种亚基蛋白（55 kDa和33 kDa）进行了化学表征。利用从两个亚基获得的部分氨基酸序列进行计算机搜索，结果表明较大的亚基属于细胞色素氧化酶亚基I蛋白家族，而较小的共价结合血红素的亚基不是细胞色素c1，似乎是细胞色素c和细胞色素氧化酶亚基II之间的融合蛋白。关于基于16-S rRNA的原核生物系统发育，结果表明，早期真细菌中已经存在与O2反应的细胞色素氧化酶（EC 1.9.3.1）的遗传信息。
