Results 141 to 150 of about 6,680 (190)
, 2009 Nitrogenase activity control in the grass-endophyte Azoarcus sp. BH72 is subjected to a posttranslational regulation, which is accompanied by covalent modification of its nitrogenase Fe-protein that was characterized here.
Oetjen, Janina
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QM/MM Studies of Nitrogenase [Elektronisk resurs]
Nitrogenase is the only enzyme that can cleave the strong triple bond in N2, making nitrogen available for biological life. Despite extensive research, the mechanism of nitrogen fixation by nitrogenase is not fully understood, partly due to the enzyme’s ...
Jiang, Hao,, Lund University.
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Annual Review of Biochemistry, 1984
Publisher Summary Nitrogen fixation ranks with photosynthesis as a process of fundamental importance to all life on earth. The biochemical process described by nitrogen fixation is the reduction of N2 to NH3, which can then be used for the synthesis of amino acids, nucleic acids, and other essential nitrogenous compounds.
V K, Shah +3 more
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Publisher Summary Nitrogen fixation ranks with photosynthesis as a process of fundamental importance to all life on earth. The biochemical process described by nitrogen fixation is the reduction of N2 to NH3, which can then be used for the synthesis of amino acids, nucleic acids, and other essential nitrogenous compounds.
V K, Shah +3 more
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2018
Biological nitrogen fixation, the conversion of dinitrogen (N2) into ammonia (NH3), stands as a particularly challenging chemical process. As the entry point into a bioavailable form of nitrogen, biological nitrogen fixation is a critical step in the global nitrogen cycle.
Nathaniel S, Sickerman +2 more
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Biological nitrogen fixation, the conversion of dinitrogen (N2) into ammonia (NH3), stands as a particularly challenging chemical process. As the entry point into a bioavailable form of nitrogen, biological nitrogen fixation is a critical step in the global nitrogen cycle.
Nathaniel S, Sickerman +2 more
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Journal of Inorganic Biochemistry, 2000
The topic, vanadium nitrogenase, is reviewed with respect to biological characteristics and findings on its structure and functions. Structural models (vanadium complexes containing ligands related to the active center in the iron-vanadium cofactor) and functional models for the reductive protonation of dinitrogen, the activation of alkynes and ...
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The topic, vanadium nitrogenase, is reviewed with respect to biological characteristics and findings on its structure and functions. Structural models (vanadium complexes containing ligands related to the active center in the iron-vanadium cofactor) and functional models for the reductive protonation of dinitrogen, the activation of alkynes and ...
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Catalysis and structure of nitrogenases
Current Opinion in Structural Biology, 2023In providing bioavailable nitrogen as building blocks for all classes of biomacromolecules, biological nitrogen fixation is an essential process for all organismic life. Only a single enzyme, nitrogenase, performs this task at ambient conditions and with ATP as an energy source.
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Dalton Transactions, 2010
In seeking to mimic the hydrogenation of N(2) to NH(3) as effected under mild conditions by the enzyme nitrogenase, three classes of known metal sulfide clusters that resemble the NFe(7)MoS(9) core of FeMo-co, the active site of nitrogenase, have been assessed theoretically.
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In seeking to mimic the hydrogenation of N(2) to NH(3) as effected under mild conditions by the enzyme nitrogenase, three classes of known metal sulfide clusters that resemble the NFe(7)MoS(9) core of FeMo-co, the active site of nitrogenase, have been assessed theoretically.
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Nitrogenase-catalyzed reactions
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1972Abstract 1. H2 evolution, N2 reduction and ATP hydrolysis, catalyzed by a particulate nitrogenase from Azotobacter vinelandii, showed similar dependence on the concentration of ATP. Higher concentrations of ATP were inhibitory. 2. Evolution of H2 by nitrogenase under the conditions studied could not be completely stopped. 3.
J C, Hwang, R H, Burris
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Derepression of nitrogenase in Azotobacter
Biochemical and Biophysical Research Communications, 1974Abstract When nitrogenase in Azotobacter vinelandii 12837 is repressed by ammonia, the derepression is accelerated by endotoxin or cyclic AMP. The phenomenon appears neither to be a consequence of accelerated ammonia utilization nor altered activity of preformed enzyme. This is a unique example of an effect of endotoxin on a procaryotic system.
J E, Lepo, O, Wyss
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