多变鱼腥蓝细菌（ATCC 29413）中固氮酶还原酶的体外激活
In vitro activation of dinitrogenase reductase from the cyanobacterium Anabaena variabilis (ATCC 29413).
作者信息
Böhm I, Halbherr A, Smaglinski S, Ernst A, Böger P
机构信息
Lehrstuhl für Physiologie und Biochemie Pflanzen, Universität Konstanz, Germany.
出版信息
J Bacteriol. 1992 Oct;174(19):6179-83. doi: 10.1128/jb.174.19.6179-6183.1992.
Abstract
Nitrogenase of the heterocystous cyanobacterium Anabaena variabilis was inactivated in vivo (S. Reich, H. Almon, and P. Böger, FEMS Microbiol. Lett. 34:53-56, 1986). Partially purified and modified (inactivated) dinitrogenase reductase (Fe-protein) of such cells was reactivated by isolated membrane fractions of A. variabilis or of Rhodospirillum rubrum, and acetylene reduction was measured. Reactivation requires ATP, Mg2+, and Mn2+. The activating principle is localized in the heterocyst and was found effective only when prepared from cells exhibiting active nitrogenase. It also restores the activity of modified Fe-protein from R. rubrum.
摘要
多变鱼腥藻这种具有异形胞的蓝细菌的固氮酶在体内被灭活（S. 赖希、H. 阿尔蒙和P. 伯格尔，《FEMS微生物学快报》34:53 - 56，1986年）。这种细胞的部分纯化且经修饰（灭活）的固氮酶还原酶（铁蛋白）可被多变鱼腥藻或深红红螺菌的分离膜组分重新激活，并测定乙炔还原情况。重新激活需要ATP、Mg²⁺和Mn²⁺。激活原理定位于异形胞，并且发现只有从表现出活性固氮酶的细胞制备时才有效。它还能恢复深红红螺菌经修饰的铁蛋白的活性。
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