An iron dioxygenase from Alcaligenes faecalis catalyzing the oxidation of pyruvic oxime to nitrite.
An enzyme which participated in the oxidation of hydroxylamine to nitrite from was partially purified Alcaligenes faecalis, and some of its properties were studied. The enzyme oxidized aerobically pyruvic oxime to nitrite in the presence of hydroxylamine or ascorbate. As molecular oxygen equimolar to nitrite formed was consumed in the enzymatic oxidation of pyruvic oxime to nitrite, the enzyme was thought to be a dioxygenase. It was an iron protein, and a reducing reagent was required to keep the iron in the ferrous state for the action of the enzyme.
Ono
Y
Y
Department of Industrial Chemistry, College of Science and Technology, Nihon University, Tokyo, Japan.
Makino
N
N
Hoshino
Y
Y
Shoji
K
K
Yamanaka
T
T
D000421:Alcaligenes / Q000201:enzymology*; D000645:Ammonium Sulfate; D007506:Iron-Sulfur Proteins / Q000302:isolation & purification / Q000378:metabolism*; D009573:Nitrites / Q000378:metabolism*; D010084:Oxidation-Reduction; D010105:Oxygenases / Q000302:isolation & purification / Q000378:metabolism*; D011422:Propionates / Q000378:metabolism*
D007506:Iron-Sulfur Proteins; D009573:Nitrites; D011422:Propionates; C003014:pyruvatoxime; D010105:Oxygenases; D000645:Ammonium Sulfate