title: The 'methylamine oxidase' system of an obligate methylotroph.
abstract: The terminal respiratory oxidase was solubilized from membranes of organism 4025, an obligate methylotroph. The partially purified oxidase is probably a cytochrome co. It does not oxidize amicyanin, but it oxidizes 'azurin' and cytochromes cH and cL. By using a complete 'methylamine oxidase' system reconstituted from pure methylamine dehydrogenase, purified oxidase and soluble blue copper proteins and cytochromes, it was confirmed that amicyanin is essential for methylamine oxidation; it could not be replaced by 'azurin' or cytochrome cH or cL. It was shown that the usual mediator between amicyanin and the oxidase is cytochrome cH, with 'azurin' able to replace it during growth at the high copper concentrations required for optimum growth of this unusual methylotroph.
authors.affiliation: Department of Biochemistry, University of Southampton, U.K.
authors.forename: K A
authors.initials: KA
authors.lastname: Auton
authors.forename: C
authors.initials: C
authors.lastname: Anthony
mesh_terms: D001400:Azurin / Q000031:analogs & derivatives / Q000378:metabolism; D001426:Bacterial Proteins; D003574:Cytochrome c Group / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000378:metabolism; D008772:Methylococcaceae / Q000201:enzymology*; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D003574:Cytochrome c Group; C017079:mauC protein, Methylobacterium extorquens; D001400:Azurin; C021567:methylamine dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors; D003576:Electron Transport Complex IV