Abstract
Abstract— 2‐Nitropropane dioxygenase (EC 1. 13. 11) of the yeast Hansenula mrakii catalyzes the oxygenative denitrification of 2‐nitropropane as follows: image The enzyme is significantly inhibited by superoxide dismutase and various scavengers for superoxide such as cytochrome c, epinephrine, thiols and polyhydric phenols. The scavengers added to the reaction mixture were oxidized or reduced. The addition of superoxide dismutase and the omission of 2‐nitropropane or oxygen prevented the oxidation and the reduction of the scavengers. The enzyme catalyzes the formation of nitrite from 2‐nitropropane by KO2 added anaerobically.One mole of NADH is bound per mole of the enzyme and predominantly the pro‐R hydrogen of bound NADH is transferred to superoxide formed enzymatically or provided externally. The enzyme shows incomplete stereospecificity for hydrogen transfer from NADH.
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