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Biosynthesis of Nitrogenase Cofactors [PDF]
Chemical Reviews, 2020 Nitrogenase harbors three distinct metal prosthetic groups that are required for its activity. The simplest one is a [4Fe-4S] cluster located at the Fe protein nitrogenase component. The MoFe protein component carries an [8Fe-7S] group called P-cluster and a [7Fe-9S-C-Mo-R-homocitrate] group called FeMo-co.
Stefan Burén +2 more
exaly +5 more sources
Electron Transfer in Nitrogenase
Chemical Reviews, 2020 Nitrogenase is the only enzyme capable of reducing N2 to NH3. This challenging reaction requires the coordinated transfer of multiple electrons from the reductase, Fe-protein, to the catalytic component, MoFe-protein, in an ATP-dependent fashion. In the last two decades, there have been significant advances in our understanding of how nitrogenase ...
Hannah L Rutledge, F Akif Tezcan
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The Spectroscopy of Nitrogenases [PDF]
Chemical Reviews, 2020 Nitrogenases are responsible for biological nitrogen fixation, a crucial step in the biogeochemical nitrogen cycle. These enzymes utilize a two-component protein system and a series of iron-sulfur clusters to perform this reaction, culminating at the FeMco active site (M = Mo, V, Fe), which is capable of binding and reducing N2 to 2NH3. In this review,
Casey Van Stappen +6 more
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Metalloclusters of the nitrogenases [PDF]
European Journal of Biochemistry, 1992 Biological nitrogen fixation, the reduction of dinitrogen to ammonia, is catalysed by nitrogenases. These enzymes are found in relatively few groups of bacteria and until recently it appeared that N2 fixation occurred by a single route involving a molybdenum-containing enzyme.
Robert R. Eady, Barry E. Smith
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Nitrogenase and homologs [PDF]
JBIC Journal of Biological Inorganic Chemistry, 2014 Nitrogenase catalyzes biological nitrogen fixation, a key step in the global nitrogen cycle. Three homologous nitrogenases have been identified to date, along with several structural and/or functional homologs of this enzyme that are involved in nitrogenase assembly, bacteriochlorophyll biosynthesis and methanogenic process, respectively.
Hu, Yilin, Ribbe, Markus W
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The photoreduction of nitrogenase [PDF]
Biochemical Journal, 1993 The photoreduction, without reductant dithionite, of N2 to NH3 or acetylene to ethylene catalysed by nitrogenase in the presence of Mg2+. ATP, eosin and NADH in the light has been established. There is an optimum NADH concentration for each particular eosin concentration.
G I Likhtenstein +3 more
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Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2013 Nitrogenase contains two unique metalloclusters: the P-cluster and the M-cluster. The assembly processes of P- and M-clusters are arguably the most complicated processes in bioinorganic chemistry. There is considerable interest in decoding the biosynthetic mechanisms of the P- and M-clusters, because these clusters are not only biologically important ...
Hu, Yilin, Ribbe, Markus W.
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Energy Transduction in Nitrogenase [PDF]
Accounts of Chemical Research, 2018 Nitrogenase is a complicated two-component enzyme system that uses ATP binding and hydrolysis energy to achieve one of the most difficult chemical reactions in nature, the reduction of N2 to NH3. One component of the Mo-based nitrogenase system, Fe protein, delivers electrons one at a time to the second component, the catalytic MoFe protein.
Edwin Antony +7 more
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High‐Pressure Synthesis of Ultra‐Incompressible Beryllium Tungsten Nitride Pernitride BeW10N14(N2)
Angewandte Chemie, EarlyView.The first ternary transition metal pernitride was synthesized in a high‐temperature high‐pressure approach starting from W2Be4N5. The structure features not only the rare structural motif of BeN6 octahedra but also dinitrogen anions. DFT calculations reveal ultra‐incompressible and metallic behavior of the new compound.
Georg Krach +7 more
wiley +2 more sources
Feedback inhibition of nitrogenase [PDF]
Journal of Bacteriology, 1981 No inhibition of nitrogenase activity by physiological levels of NH4+ or carbamyl phosphate was observed in extracts of Azotobacter vinelandii. All of the 15N2 reduced by cultures which received no NH4+ was found in the cells. By contrast, more than 95% of the 15N2 reduced by cultures which had been given NH4+ was found in the medium.
Winston J. Brill +2 more
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