The oxidation of nicotinic acid by Pseudomonas ovalis Chester. The terminal oxidase.
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.
D001386:Azides / Q000494:pharmacology; D002248:Carbon Monoxide; D002462:Cell Membrane / Q000201:enzymology; D002473:Cell Wall / Q000201:enzymology; D003486:Cyanides / Q000494:pharmacology; D003574:Cytochrome c Group / Q000378:metabolism; D003580:Cytochromes / Q000378:metabolism; D004579:Electron Transport; D009243:NAD; D009539:Nicotinic Acids / Q000378:metabolism*; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology / Q000378:metabolism*; D013057:Spectrum Analysis; D013386:Succinates / Q000378:metabolism
D001386:Azides; D003486:Cyanides; D003574:Cytochrome c Group; D003580:Cytochromes; D009539:Nicotinic Acids; D013386:Succinates; D009243:NAD; D002248:Carbon Monoxide; D010088:Oxidoreductases