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. 1972 Sep;129(3):755–761. doi: 10.1042/bj1290755

The oxidation of nicotinic acid by Pseudomonas ovalis Chester. The terminal oxidase

M V Jones 1, D E Hughes 1
PMCID: PMC1174177  PMID: 4349118

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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