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The terminal respiratory chain of the methylotrophic bacterium Methylophilus methylotrophus
Author(s) -
Carver Mark A.,
Jones Colin W.
Publication year - 1983
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(82)80599-1
Subject(s) - chemistry , terminal (telecommunication) , biochemistry , respiratory chain , chain (unit) , stereochemistry , physics , enzyme , computer science , telecommunications , astronomy
Cytochrome oxidase o has been isolated from the obligately aerobic, methylotrophic bacterium Methylophilus methylotrophus in the form of a cytochrome c L ‐ o complex. The latter is comprised of cytochrome c L ( M r 21 000) and cytochrome o ( M r 29 000) in a 1–2:1 ratio, possibly in association with one or more minor polypeptides; the complex exhibits a high ascorbate‐TMPD oxidase activity which is inhibited non‐competitively by cyanide ( K i ≈ 2 μM). In contrast, the oxidation of methanol by whole cells is inhibited uncompetitively by cyanide ( K i ≈4 μM), thus indicating the involvement in methanol oxidation of cytochrome oxidase aa 3 rather than o .