title: Purification and properties of a copper-containing nitrite reductase from a denitrifying bacterium, Alcaligenes faecalis strain S-6.
abstract: A copper-containing nitrite reductase was purified and crystallized from a potent denitrifying bacterium, Alcaligenes faecalis strain S-6. The enzyme was composed of 4 subunits with a molecular weight of about 30,000, each containing 1 atom of Cu2+. Nitric oxide was identified as a main reduction product from nitrite in the enzyme-catalyzed reaction. The enzyme activity was inhibited strongly by KCN but only slightly by sulfhydryl reagents such as p-chloromercuribenzoate and N-ethylmaleimide.
mesh_terms: D000421:Alcaligenes / Q000201:enzymology*; D003300:Copper; D003461:Crystallography; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D007700:Kinetics; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification*; D009572:Nitrite Reductases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D013057:Spectrum Analysis
chemical_list: D003300:Copper; D009247:NADH, NADPH Oxidoreductases; D009572:Nitrite Reductases