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血红蛋白中结合态双原子氧对氮氧化物的氧化作用。

Oxidation of nitrogen oxides by bound dioxygen in hemoproteins.

作者信息

Doyle M P, Hoekstra J W

出版信息

J Inorg Biochem. 1981 Jul;14(4):351-8. doi: 10.1016/s0162-0134(00)80291-3.

DOI:10.1016/s0162-0134(00)80291-3
PMID:7276933
Abstract

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.

摘要

一氧化氮在氮的高级氧化物中,在与氧结合的血红蛋白氧化反应中的反应活性和效率方面独具特色。三氧化二氮可作为一氧化氮供体,但四氧化二氮不具有类似的反应活性。文中详细介绍了一氧化氮转化为硝酸盐的化学计量转化过程,在此过程中,肌红蛋白或血红蛋白伴随氧化生成相应的铁(III)血红蛋白,包括对与氧结合的肌红蛋白一氧化氮氧化反应速率常数的估计,以及游离氧对一氧化氮氧化化学计量和速率的影响。文中还提供了证据以确立一氧化氮与铁(II)结合的双氧直接结合时的氧化机制。

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