Purification and characterization of nitrite-oxidizing enzyme from heterotrophic Bacillus badius 1-73, with special concern to catalase.
Nitrite-oxidizing enzyme I (NiOx I) was purified from a heterotrophic bacterium, Bacillus badius I-73. The enzyme was a homotetramer of a heme-containing peptide, and was similar to catalases from various sources in its N-terminal amino acid sequence. The purified enzyme also catalyzed H2O2 degradation. The nitrite oxidation reaction required ascorbic acid and oxygen. Successive H2O2 feeding could be substituted for ascorbic acid. These indicated that NiOx I is a catalase and nitrite was oxidized by a peroxidase-like reaction.
Sakai
K
K
Department of Applied Chemistry, Faculty of Engineering, Oita University, Japan. sakai@cc.oita-u.ac.jp
Nisijima
H
H
Ikenaga
Y
Y
Wakayama
M
M
Moriguchi
M
M
D000595:Amino Acid Sequence; D001205:Ascorbic Acid / Q000737:chemistry / Q000378:metabolism; D001407:Bacillus / Q000201:enzymology*; D002374:Catalase / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D009573:Nitrites / Q000378:metabolism*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000737:chemistry / Q000378:metabolism; D010544:Peroxidases / Q000302:isolation & purification* / Q000378:metabolism*
D009573:Nitrites; D006861:Hydrogen Peroxide; D010544:Peroxidases; C425563:nitrite-oxidizing enzyme I; D002374:Catalase; D001205:Ascorbic Acid; D010100:Oxygen