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Yasufumi Ono, Naozumi Makino, Yoshiko Hoshino, Kazuo Shoji, Tateo Yamanaka, An iron dioxygenase from Alcaligenes faecalis catalyzing the oxidation of pyruvic oxime to nitrite, FEMS Microbiology Letters, Volume 139, Issue 2-3, June 1996, Pages 103–108, https://doi.org/10.1111/j.1574-6968.1996.tb08187.x
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Abstract
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.