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Purification, and some molecular and enzymatic features of a novel ccb ‐type cytochrome c oxidase from a microaerobic denitrifier, Magnetospirillum magnetotacticum
Author(s) -
Tamegai Hideyuki,
Fukumori Yoshihiro
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00500-1
Subject(s) - cytochrome c oxidase , enzyme , heme a , cytochrome , biochemistry , electron transport complex iv , oxidase test , chemistry , heme , cytochrome c , mitochondrion
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.