title: Characterization of a multi-copper enzyme, nitrous oxide reductase, from Rhodobacter sphaeroides f. sp. denitrificans.
abstract: The nitrous oxide reductase from the photodenitrifier, Rhodobacter sphaeroides f. sp. denitrificans, has been purified. The enzyme is composed of two identical subunits of 66 kDa, and contains four copper atoms per subunit. Copper supplementation of the medium resulted in a 3.5-fold increase in the enzyme yield with doubly enhanced specific activity. The activity of the purified nitrous oxide reductase was completely inhibited by 100 microM zinc ions.
authors.affiliation: Department of Applied Biological Chemistry, The University of Tokyo, Bunkyo-ku, Tokyo, 113-8657, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Sato
authors.forename: A
authors.initials: A
authors.lastname: Okubo
authors.forename: S
authors.initials: S
authors.lastname: Yamazaki
mesh_terms: D003300:Copper / Q000737:chemistry*; D008970:Molecular Weight; D010088:Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D012242:Rhodobacter sphaeroides / Q000201:enzymology*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D003300:Copper; D010088:Oxidoreductases; C022763:nitrous oxide reductase