Abstract
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.
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