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黄嘌呤氧化酶同时还原亚硝酸盐和氧气生成过氧亚硝酸根。

Peroxynitrite formation from the simultaneous reduction of nitrite and oxygen by xanthine oxidase.

作者信息

Millar Timothy M

机构信息

Xanthine Oxidase Research Group, School of Health, University of Bath, Claverton Down, Bath BA2 7AY, UK.

出版信息

FEBS Lett. 2004 Mar 26;562(1-3):129-33. doi: 10.1016/S0014-5793(04)00218-2.

Abstract

One electron reductions of oxygen and nitrite by xanthine oxidase form peroxynitrite. The nitrite and oxygen reducing activities of xanthine oxidase are regulated by oxygen with K(oxygen) 26 and 100 microM and K(nitrite) 1.0 and 1.1 mM with xanthine and NADH as donor substrates. Optimal peroxynitrite formation occurs at 70 microM oxygen with purine substrates. Kinetic parameters: V(max) approximately 50 nmol/min/mg and K(m) of 22, 36 and 70 microM for hypoxanthine, pterin and nitrite respectively. Peroxynitrite generation is inhibited by allopurinol, superoxide dismutase and diphenylene iodonium. A role for this enzyme activity can be found in the antibacterial activity of milk and circulating xanthine oxidase activity.

摘要

黄嘌呤氧化酶对氧和亚硝酸盐的单电子还原形成过氧亚硝酸盐。以黄嘌呤和NADH作为供体底物时,黄嘌呤氧化酶的亚硝酸盐还原活性和氧还原活性受氧调节,氧的K值分别为26和100微摩尔,亚硝酸盐的K值分别为1.0和1.1毫摩尔。在有嘌呤底物存在的情况下,70微摩尔的氧浓度时过氧亚硝酸盐生成最为理想。动力学参数:最大反应速度(V(max))约为50纳摩尔/分钟/毫克,次黄嘌呤、蝶呤和亚硝酸盐的米氏常数(K(m))分别为22、36和70微摩尔。别嘌呤醇、超氧化物歧化酶和二苯碘鎓可抑制过氧亚硝酸盐的生成。这种酶活性在牛奶的抗菌活性以及循环黄嘌呤氧化酶活性中发挥作用。

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