In cell-free extracts of Pseudomonas ovalis nicotinic acid oxidase is confined to the wallmembrane fraction. It is associated with an electron-transport chain comprising b- and c-type cytochromes only, differing proportions of which are reduced by nicotinate and NADH. CO difference-spectra show two CO-binding pigments, cytochrome o (absorption maximum at 417nm) and another component absorbing maximally at 425nm. Cytochrome o is not reduced by NADH or by succinate but is by nicotinate, which can also reduce the ‘425’ CO-binding pigment. The effects of inhibitors of terminal oxidation support the idea of two terminal oxidases and a scheme involving the ‘425’ CO-binding pigment and the other components of the electron-transport chain is proposed.
Research Article|September 01 1972
The oxidation of nicotinic acid by Pseudomonas ovalis Chester. The terminal oxidase
M. V. Jones;
Biochem J (1972) 129 (3): 755-761.
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M. V. Jones, D. E. Hughes; The oxidation of nicotinic acid by Pseudomonas ovalis Chester. The terminal oxidase. Biochem J 1 September 1972; 129 (3): 755–761. doi: https://doi.org/10.1042/bj1290755
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