Yamanaka T, Fukumori Y, Tanaka Y
Orig Life. 1984;14(1-4):739-46. doi: 10.1007/BF00933729.
Cytochrome aa3 (cytochrome c oxidase) and cytochrome c were purified from Nitrobacter agilis, and some of their properties were compared with those of the respective counterparts of eukaryote from the evolutionary point of view. N. agilis cytochrome aa3 has many functional and structural properties similar to those of eukaryotic cytochrome aa3, although its molecule is composed of only two kinds of subunits unlike the eukaryotic cytochrome which is composed of 7 kinds of subunits. N. agilis cytochrome c is homologous to eukaryotic cytochrome c; 50 amino acid residues of the bacterial cytochrome c are identical with those of horse cytochrome c. It reacts with yeast cytochrome c peroxidase as rapidly as eukaryotic cytochrome c does. So far as based on the molecular features of cytochromes aa3 and c, N. agilis appears to be one of the organisms which may link in evolution prokaryote to eukaryote.
从活跃硝化杆菌中纯化出细胞色素aa3（细胞色素c氧化酶）和细胞色素c，并从进化的角度将它们的一些特性与真核生物中相应的细胞色素进行了比较。活跃硝化杆菌细胞色素aa3具有许多与真核细胞色素aa3相似的功能和结构特性，尽管其分子仅由两种亚基组成，这与由7种亚基组成的真核细胞色素不同。活跃硝化杆菌细胞色素c与真核细胞色素c同源；细菌细胞色素c的50个氨基酸残基与马细胞色素c的相同。它与酵母细胞色素c过氧化物酶的反应速度与真核细胞色素c一样快。就细胞色素aa3和c的分子特征而言，活跃硝化杆菌似乎是在进化过程中可能连接原核生物和真核生物的生物之一。
