title: The methylamine oxidizing system of Pseudomonas AM1 reconstituted with purified components.
abstract: The electron transport system coupled to the oxidation of methylamine in Pseudomonas AM1 was investigated by reconstituting it from the highly purified components. A mixture of methylamine dehydrogenase, cytochrome cH and cytochrome c oxidase (= cytochrome aa3) actively oxidized methylamine (161 mol of O2 consumed/mol of heme a of cytochrome c oxidase X min). In this system, addition of amicyanin did not affect the oxygen consumption rate. The oxygen consumption rate of the cell-free extract prepared from the cells cultivated in a copper-deficient medium was directly proportional to the amount of amicyanin added, and extrapolation to zero copper concentration gave a value of 28 mol of O2 consumed/mol of heme a of cytochrome c oxidase X min. These results suggest that methylamine oxidation in the bacterium can occur at least to some extent without participation of amicyanin.
mesh_terms: D001426:Bacterial Proteins; D003300:Copper / Q000494:pharmacology; D003574:Cytochrome c Group / Q000378:metabolism; D004579:Electron Transport / Q000187:drug effects; D008667:Metalloproteins / Q000494:pharmacology; D008744:Methylamines / Q000378:metabolism*; D010084:Oxidation-Reduction; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism; D010101:Oxygen Consumption / Q000187:drug effects; D011549:Pseudomonas / Q000254:growth & development / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D003574:Cytochrome c Group; D008667:Metalloproteins; D008744:Methylamines; C017079:mauC protein, Methylobacterium extorquens; D003300:Copper; C027451:methylamine; C021567:methylamine dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors