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Title: Selective one-electron reduction of Nitrosomonas europaea hydroxylamine oxidoreductase with nitric oxide. Author: Cabail MZ, Pacheco AA. Journal: Inorg Chem; 2003 Jan 27; 42(2):270-2. PubMed ID: 12693206. Abstract: Hydroxylamine oxidoreductase (HAO) from the autotrophic bacterium Nitrosomonas europaea catalyzes the 4-e- oxidation of NH2-OH to NO2-. The e- are transferred from NH2OH to an unusual 5-coordinate heme known as P460, which is the active site of HAO, and from there to an array of seven c-type hemes. NO., generated by laser flash photolysis of N,N'-bis(carboxymethyl)-N,N'-dinitroso-1,4-phenylenediamine, is found to act as a 1-e- donor to HAO. Most likely NO. binds P460 to yield a [Fe(NO)]6 moiety, which then hydrolyzes to give the reduced enzyme and NO2-. The [Fe(NO)]6 moiety is also a plausible final intermediate in the oxidation of NH2OH.[Abstract] [Full Text] [Related] [New Search]