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假单胞菌属一种细胞内蛋白质对锰的氧化作用。

Manganese oxidation by an intracellular protein of a Pseudomonas species.

作者信息

Jung W K, Schweisfurth R

出版信息

Z Allg Mikrobiol. 1979;19(2):107-15.

PMID:39383
Abstract

Cultures of a Pseudomonas sp. strain MnB 1 produce an intracellular, manganese oxidizing protein (abbrev. as Mn ox. protein) during the stationary phase of growth. This protein is heat labile, can be inactivated by protease and has a pH-optimum for manganese oxidation at pH 7.0. Mn2+ is oxidized only at concentrations below 3-10(-5) M. The occurrence of the protein is not dependent on the presence of Mn2+, but is clearly related to the cessation of growth after the end of the exponential growth phase. Oxygen, coenzymes, and low molecular weight components of the cell extract seem not to be involved in the reaction as electron acceptors for the oxidation of Mn2+. Continued manganese oxidation by Mn ox. protein results in a progressive decrease in activity which corresponds to the amount of formed manganese oxide.

摘要

假单胞菌属MnB 1菌株的培养物在生长稳定期产生一种细胞内锰氧化蛋白(简称为锰氧化蛋白)。该蛋白对热不稳定,可被蛋白酶灭活,在pH 7.0时锰氧化的最适pH值为7.0。只有在浓度低于3×10⁻⁵ M时,Mn²⁺才会被氧化。该蛋白的产生不依赖于Mn²⁺的存在,但明显与指数生长期结束后生长的停止有关。氧气、辅酶和细胞提取物中的低分子量成分似乎不参与作为Mn²⁺氧化电子受体的反应。锰氧化蛋白持续进行锰氧化会导致活性逐渐降低,这与形成的锰氧化物量相对应。

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