Haltia T, Puustinen A, Finel M
Department of Medical Chemistry, University of Helsinki.
Eur J Biochem. 1988 Mar 15;172(3):543-6. doi: 10.1111/j.1432-1033.1988.tb13923.x.
The presence of a third polypeptide subunit in Paracoccus cytochrome c oxidase is demonstrated. This protein (apparent molecular mass 23 kDa) binds dicyclohexylcarbodiimide in membranes of aerobically grown bacteria and in the purified enzyme. The N-terminal amino-acid sequence of this dicyclohexylcarbodiimide-binding protein is identical to the deduced sequence of the COIII gene product [Raitio et al. (1987) EMBO J. 6, 2825-2833]. We conclude that the aa3-type oxidase in Paracoccus is composed of at least three subunits, which correspond to the three mitochondrially coded polypeptides in the eukaryotic enzyme.
已证实副球菌细胞色素c氧化酶中存在第三种多肽亚基。这种蛋白质（表观分子量23 kDa）在需氧生长细菌的膜和纯化的酶中与二环己基碳二亚胺结合。这种二环己基碳二亚胺结合蛋白的N端氨基酸序列与COIII基因产物的推导序列相同[拉蒂奥等人（1987年），《欧洲分子生物学组织杂志》6，2825 - 2833]。我们得出结论，副球菌中的aa3型氧化酶至少由三个亚基组成，这三个亚基与真核酶中由线粒体编码的三种多肽相对应。
