title: The terminal oxidase in the marine bacterium Pseudomonas nautica 617.
abstract: The molecular properties of a novel membrane quinol oxidase from the marine bacterium Pseudomonas nautica 617 are presented. The protein contains 2b hemes/mole which may be distinguished by EPR spectroscopy but not by optical spectroscopy and electrochemistry. Respiration, though being cyanide insensitive, is not inhibited by carbon monoxide and oxygen reduction is carried out only half-way with production of hydrogen peroxide. The terminal oxidase represents, therefore, a unique example in the large family of terminal oxidases known up to date.
authors.affiliation: Centre d'Oceanologie de Marseille, CNRS UA41, Faculte' des Sciences de Luminy, France.
authors.forename: H
authors.initials: H
authors.lastname: Simpson
authors.forename: M
authors.initials: M
authors.lastname: Denis
authors.forename: F
authors.initials: F
authors.lastname: Malatesta
mesh_terms: D006861:Hydrogen Peroxide / Q000378:metabolism; D010088:Oxidoreductases / Q000737:chemistry* / Q000502:physiology*; D010100:Oxygen / Q000378:metabolism; D011549:Pseudomonas / Q000201:enzymology*; D014871:Water Microbiology
chemical_list: D006861:Hydrogen Peroxide; D010088:Oxidoreductases; D010100:Oxygen