来自反硝化副球菌GB17的一种新型非血红素铁羟胺氧化酶的生化特性
The biochemical characterization of a novel non-haem-iron hydroxylamine oxidase from Paracoccus denitrificans GB17.
作者信息
Moir J W, Wehrfritz J M, Spiro S, Richardson D J
机构信息
School of Biological Sciences, University of East Anglia, Norwich, U.K.
出版信息
Biochem J. 1996 Nov 1;319 ( Pt 3)(Pt 3):823-7. doi: 10.1042/bj3190823.
Abstract
The characterization of the hydroxylamine oxidase from the heterotrophic nitrifier Paracoccus denitrificans GB17 indicates the enzyme to be entirely distinct from the hydroxylamine oxidase from the autotrophic nitrifier Nitrosomonas europaea. Hydroxylamine oxidase from P. denitrificans contains three to five non-haem, non-iron-sulphur iron atoms as prosthetic groups, predominantly co-ordinated by carboxylate ligands. The interaction of the enzyme with the electron-accepting proteins cytochrome C556 and pseudoazurin is mainly hydrophobic. The catalytic mechanism of hydroxylamine oxidase from P. denitrificans is different from the enzyme from N. europaea because the production of nitrite by the former requires molecular oxygen. Under anaerobic conditions the enzyme makes nitrous oxide as a sole product.
摘要
对异养硝化菌反硝化副球菌GB17中羟胺氧化酶的特性分析表明，该酶与自养硝化菌欧洲亚硝化单胞菌中的羟胺氧化酶完全不同。反硝化副球菌中的羟胺氧化酶含有三到五个非血红素、非铁硫铁原子作为辅基，主要由羧酸盐配体配位。该酶与电子受体蛋白细胞色素C556和假蓝铜蛋白的相互作用主要是疏水作用。反硝化副球菌中羟胺氧化酶的催化机制与欧洲亚硝化单胞菌中的酶不同，因为前者产生亚硝酸盐需要分子氧。在厌氧条件下，该酶仅产生一氧化二氮作为产物。
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