2018
DOI: 10.1016/j.cbpa.2018.08.011
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Control of electron transfer in nitrogenase

Abstract: The bacterial enzyme nitrogenase achieves the reduction of dinitrogen (N) to ammonia (NH) utilizing electrons, protons, and energy from the hydrolysis of ATP. Building on earlier foundational knowledge, recent studies provide molecular-level details on how the energy of ATP hydrolysis is utilized, the sequencing of multiple electron transfer events, and the nature of energy transduction across this large protein complex. Here, we review the state of knowledge about energy transduction in nitrogenase.

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Cited by 46 publications
(40 citation statements)
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“…The heterotetramer contains a [4Fe‐4S] cluster and two ATP binding sites. The dinitrogenase reductase is a homodimer of approximately 60–70 kDa, and the subunit is encoded by NifH , which acts to transfer electrons from the external electron donors (ferredoxins or flavodoxins) to dinitrogenase . Nitrogenase conversion efficiency is lower than [FeFe]‐hydrogenase and [NiFe]‐hydrogenase .…”
Section: Hydrogen Synthesizing Enzymes In Microalgaementioning
confidence: 99%
“…The heterotetramer contains a [4Fe‐4S] cluster and two ATP binding sites. The dinitrogenase reductase is a homodimer of approximately 60–70 kDa, and the subunit is encoded by NifH , which acts to transfer electrons from the external electron donors (ferredoxins or flavodoxins) to dinitrogenase . Nitrogenase conversion efficiency is lower than [FeFe]‐hydrogenase and [NiFe]‐hydrogenase .…”
Section: Hydrogen Synthesizing Enzymes In Microalgaementioning
confidence: 99%
“…N 2 fixation requires a significant number of metalloproteins of the photosynthetic and respiratory metabolism, which have high Fe and Cu requirements [40,144,145,146], to provide energy and electrons to this essential biological process for the nitrogen cycle [144]. Nitrogenases contain 38 atoms of Fe and either two Mo or two V atoms [147,148]. Other metalloenzymes are crucial to manage efficiently reactive oxygen species generated during the metabolism of heterocysts, while some metalloproteins are especially important in Fe storage, which is the most required transition metal in heterocysts [40,144,149].…”
Section: Cyanobacteria and Heterocystsmentioning
confidence: 99%
“…The dinitrogenase reductase is also known as Fe protein and contains one [4Fe–4S] cluster and two ATP binding sites. In turn, the dinitrogenase is also called MoFe protein (in Mo nitrogenases), VFe protein (in V nitrogenases) or FeFe protein (in Fe nitrogenases) and houses an electron-transfer P cluster as well as the active-site metal cofactor FeMo-co, FeV-co, or FeFe-co, respectively [148]. All nitrogenases consume high amounts of ATP and reducing equivalents, thus, heterocysts keep the respiratory and, partially, the photosynthetic electron transport chains around the PSI to support photophosphorylation and reduction of Fd in order to provide nitrogenase enzymes with energy and electrons [85].…”
Section: Metalloproteins In N2 Fixation and H2 Metabolismmentioning
confidence: 99%
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“…Schematic structure of nitrogenase, where R and R* are the ligands. The figure was rearranged from Seefeldt et al[23].…”
mentioning
confidence: 99%