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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.
Robert H. Burris, J.C. Hwang
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Nitrogenase: standing at the crossroads
Current Opinion in Chemical Biology, 2000Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia, which is central to the process of biological nitrogen fixation. Recent progress towards establishing the mechanism of action of this complex metalloenzyme reflects the contributions of a combination of structural, biochemical, spectroscopic, synthetic and theoretical ...
Rees, Douglas C., Howard, James B.
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Nitrogenase Bioelectrochemistry for Synthesis Applications.
Accounts of Chemical Research, 2019The fixation of atmospheric dinitrogen to ammonia by industrial technologies (such as the Haber Bosch process) has revolutionized humankind. In contrast to industrial technologies, a single enzyme is known for its ability to reduce or "fix" dinitrogen ...
Ross D. Milton, S. Minteer
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Mechanism of Molybdenum Nitrogenase
Chemical Reviews, 1996AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
B. K. Burgess, D. J. Lowe
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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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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.
Orville Wyss, Joe E. Lepo
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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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Nature Microbiology, 2018
An alternative nitrogenase enzyme that only utilizes iron as its cofactor is shown to reduce carbon dioxide while actively fixing dinitrogen, so that it simultaneously produces ammonium, hydrogen and methane.
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An alternative nitrogenase enzyme that only utilizes iron as its cofactor is shown to reduce carbon dioxide while actively fixing dinitrogen, so that it simultaneously produces ammonium, hydrogen and methane.
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Crystallization of Nitrogenase Proteins
2018Nitrogenase is the only known enzymatic system capable of reducing atmospheric dinitrogen to ammonia. This unique reaction requires tightly choreographed interactions between the nitrogenase component proteins, the molybdenum-iron (MoFe)- and iron (Fe)-proteins, as well as regulation of electron transfer between multiple metal centers that are only ...
Wenke, Belinda B. +2 more
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Cluster assembly in nitrogenase
Essays in Biochemistry, 2017The versatile enzyme system nitrogenase accomplishes the challenging reduction of N2and other substrates through the use of two main metalloclusters. For molybdenum nitrogenase, the catalytic component NifDK contains the [Fe8S7]-core P-cluster and a [MoFe7S9C-homocitrate] cofactor called the M-cluster.
Nathaniel S. Sickerman +4 more
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