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由钒还原细菌分泌的钒结合蛋白。

Vanadium-binding protein excreted by vanadate-reducing bacteria.

作者信息

Antipov A N, Lyalikova N N, L'vov N P

机构信息

N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia.

出版信息

IUBMB Life. 2000 Feb;49(2):137-41. doi: 10.1080/15216540050022467.

Abstract

A vanadium-binding protein was isolated from the culture medium of the vanadium-reducing bacterium Pseudomonas isachenkovii by utilizing vanadate as the terminal electron acceptor upon anaerobic respiration. The protein was associated with vanadium at a molar ratio of approximately 1:20. It was purified to homogeneity and separated into three components by treatment with 1 M HCl followed by gel filtration: a protein, a vanadium-binding ligand, and inorganic vanadium. Electron paramagnetic resonance analysis showed that vanadium was associated with the protein in the 4+ oxidation state. The distribution of vanadium within the cell was studied by electron microscopy and x-ray microanalysis of P. isachenkovii cells. The results suggest that vanadium, accumulated in special swells on the surface of the cell membranes, is reduced and excreted to the medium.

摘要

通过利用钒酸盐作为厌氧呼吸时的末端电子受体,从钒还原菌伊萨琴科夫假单胞菌(Pseudomonas isachenkovii)的培养基中分离出一种钒结合蛋白。该蛋白与钒的摩尔比约为1:20。它被纯化至同质,并通过用1 M盐酸处理后进行凝胶过滤分离为三个组分:一种蛋白质、一种钒结合配体和无机钒。电子顺磁共振分析表明,钒以4+氧化态与该蛋白结合。通过对伊萨琴科夫假单胞菌细胞进行电子显微镜和X射线微分析研究了钒在细胞内的分布。结果表明,积累在细胞膜表面特殊肿胀部位的钒被还原并排泄到培养基中。

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