Purification, and some molecular and enzymatic features of a novel ccb‐type cytochrome c oxidase from a microaerobic denitrifier, Magnetospirillum magnetotacticum

FEBS Letters

Fukumori, Yoshihiro¹  Tamegai, Hideyuki¹ 

[1] Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 227, Japan

关键词: Cytochrome c oxidase;    Microaerobic respiration;    Magnetic bacterium;    Magnetospirillum magnetotacticum;   

DOI  :  10.1016/0014-5793(94)00500-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A novel ccb-type cytochrome c oxidase was purified from the magnetic bacterium, Magnetospirillum magnetotacticum MS-1. The enzyme was composed of three subunits with M _r's of 43,000, 34,000 and 28,000, respectively, and contained 0.91 mol of protoheme, 2.0 mol of heme c and 0.70 g atom of copper per mol of minimal structural unit. One mol of enzyme oxidized 187 mol of horse heart ferrocytochrome c and 34.4 mol of M. magnetotacticum ferrocytochrome c ₅₅₀/s. The cytochrome c oxidase activity of the enzyme was 50% inhibited by 12 μM KCN. The enzyme seems to function as the terminal oxidase in microaerobic respiration.

【 授权许可】

Unknown