Oxidation of nitrogen oxides by bound dioxygen in hemoproteins.
Nitric oxide is unique among the higher oxides of nitrogen in its reactivity and efficiency for the oxidation of oxygen-bound hemoproteins. Dinitrogen trioxide serves as a nitric oxide donor, but dinitrogen tetroxide does not exhibit similar reactivity. Details are provided of the stoichiometric transformation through which nitric oxide is converted to nitrate with accompanying oxidation of myoglobin or hemoglobin to the corresponding iron(III) hemoprotein, including an estimate of the rate constant for nitric oxide oxidation of oxygen-associated myoglobin and the effect of unassociated oxygen on the stoichiometry and rates for nitric oxide oxidation. Evidence is presented to establish the mechanism of oxidation in the direct combination of nitric oxide with iron(II)-bound dioxygen.
D000818:Animals; D006441:Hemoglobin A; D006736:Horses; D006801:Humans; D007700:Kinetics; D009206:Myocardium; D009211:Myoglobin; D009569:Nitric Oxide; D009589:Nitrogen Oxides; D010084:Oxidation-Reduction; D010108:Oxyhemoglobins
D009211:Myoglobin; D009589:Nitrogen Oxides; D010108:Oxyhemoglobins; C017595:oxymyoglobin; C031701:nitrogen trioxide; D009569:Nitric Oxide; D006441:Hemoglobin A