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首页> 外文期刊>Journal of bacteriology >Complementary functioning of the component proteins of nitrogenase from several bacteria.
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Complementary functioning of the component proteins of nitrogenase from several bacteria.

机译:来自几种细菌的固氮酶组成蛋白的互补功能。

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The nitrogenase proteins from eight organisms have been highly purified, and a survey of their cross-reactions shows that the nitrogenase proteins from a wide variety of organisms can interact with one another. An active cross-reaction is the complementary functioning of the MoFe protein and the Fe protein from different organisms. Of 64 possible combinations of component proteins, 8 yielded homologous nitrogenases (components from the same organism); 45 of the 56 possible heterologous crosses generated active hybrid nitrogenases; 4 heterologous crosses yielded no measurable nitrogenase activity but did form inactive tight-binding complexes; 6 crosses did not give measurable activity; and 1 cross was not made. All these crosses were assayed for acetylene reduction, and some also were assayed for ammonia formation, hydrogen evolution, and ATP hydrolysis activity. The activity generated by combining two complementary heterologous nitrogenase components depended on pH, component ratio, and protein concentration, the same factors that determine the activity of homologous nitrogenases. However, several crosses showed an unusual dependency on component ratio and protein concentration, and some cross-reactions showed interesting ATP hydrolysis activity.
机译:来自八个生物体的固氮酶蛋白已经过高度纯化,对它们的交叉反应的调查显示,来自多种生物体的固氮酶蛋白可以彼此相互作用。活跃的交叉反应是来自不同生物的MoFe蛋白和Fe蛋白的互补功能。在成分蛋白质的64种可能组合中,有8种产生了同源的固氮酶(来自同一生物的成分); 56个可能的异源杂交中有45个产生了活性杂交固氮酶; 4个异源杂交没有产生可测量的固氮酶活性,但确实形成了无活性的紧密结合复合物; 6个十字架没有给出可衡量的活动;并且没有做出1个十字架。分析所有这些杂交的乙炔还原,还分析一些杂交的氨形成,析氢和ATP水解活性。通过组合两个互补的异源固氮酶组分产生的活性取决于pH,组分比率和蛋白质浓度,这是决定同源固氮酶活性的相同因素。但是,一些杂交显示出对组分比例和蛋白质浓度的非同寻常的依赖性,并且一些交叉反应显示出有趣的ATP水解活性。

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