Electron Transfer to Nitrogenase in Different Genomic and Metabolic Backgrounds

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Electron Transfer and Substrate Reduction in Nitrogenase

.....................................................................................................53 Introduction ................................................................................................54 Materials and Methods ...............................................................................58 Results ........................................................................

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Electron transfer and half-reactivity in nitrogenase.

Nitrogenase is a globally important enzyme that catalyses the reduction of atmospheric dinitrogen into ammonia and is thus an important part of the nitrogen cycle. The nitrogenase enzyme is composed of a catalytic molybdenum-iron protein (MoFe protein) and a protein containing an [Fe4-S4] cluster (Fe protein) that functions as a dedicated ATP-dependent reductase. The current understanding of el...

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Electron transfer precedes ATP hydrolysis during nitrogenase catalysis.

The biological reduction of N2 to NH3 catalyzed by Mo-dependent nitrogenase requires at least eight rounds of a complex cycle of events associated with ATP-driven electron transfer (ET) from the Fe protein to the catalytic MoFe protein, with each ET coupled to the hydrolysis of two ATP molecules. Although steps within this cycle have been studied for decades, the nature of the coupling between ...

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Electron transfer in nitrogenase analyzed by Marcus theory: evidence for gating by MgATP.

Nitrogenase-catalyzed substrate reduction reactions require electron transfer between two component proteins, the iron (Fe) protein and the molybdenum-iron (MoFe) protein, in a reaction that is coupled to the hydrolysis of MgATP. In the present work, electron transfer (Marcus) theory has been applied to nitrogenase electron transfer reactions to gain insights into possible roles for MgATP in th...

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The fixABCX genes in Rhodospirillum rubrum encode a putative membrane complex participating in electron transfer to nitrogenase.

In our efforts to identify the components participating in electron transport to nitrogenase in Rhodospirillum rubrum, we used mini-Tn5 mutagenesis followed by metronidazole selection. One of the mutants isolated, SNT-1, exhibited a decreased growth rate and about 25% of the in vivo nitrogenase activity compared to the wild-type values. The in vitro nitrogenase activity was essentially wild typ...

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ژورنال

عنوان ژورنال: Journal of Bacteriology

سال: 2018

ISSN: 0021-9193,1098-5530

DOI: 10.1128/jb.00757-17