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Nitrogenase-catalyzed reactions

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1972
Abstract 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
openaire   +2 more sources

MOLYBDENUM IN NITROGENASE

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
openaire   +2 more sources

Mimicking nitrogenase

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.
openaire   +2 more sources

Vanadium nitrogenase

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 ...
openaire   +2 more sources

Nitrogenase Bioelectrochemistry for Synthesis Applications.

Accounts of Chemical Research, 2019
The 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
semanticscholar   +1 more source

Mechanism of Molybdenum Nitrogenase

Chemical Reviews, 1996
Barbara K., Burgess, David J., Lowe
exaly   +3 more sources

Nitrogenases without molybdenum

Trends in Biochemical Sciences, 1989
For 50 years molybdenum had been considered to have an indispensable catalytic function for nitrogen fixation. Two nitrogenases recently isolated from the bacterium Azotobacter have changed this view. One is a vanadium-containing enzyme and the other lacks both molybdenum and vanadium. Similar nitrogenases may occur in other nitrogen-fixing organisms.
openaire   +2 more sources

Nitrogenase Bioelectrocatalysis

ECS Meeting Abstracts, 2019
Nitrogenase is the only enzyme capable of nitrogen reduction to ammonia. This talk will discuss cobaltocene and methyl viologen mediation schemes for MoFe and VFe nitrogenase, as well as strategies for nitrogenase bioelectrocatalysis in air. Bioelectrocatalysis of proton reduction, azide reduction, nitrite reduction, nitrogen reduction, and carbon ...
openaire   +1 more source

The Critical E4 State of Nitrogenase Catalysis.

Biochemistry, 2018
The reaction catalyzed by the nitrogenase enzyme involves breaking the stable triple bond of the dinitrogen molecule and is consequently considered among the most challenging reactions in biology.
M. Rohde   +4 more
semanticscholar   +1 more source

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