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Nitrogenase

Known as: Dinitrogenase, Nitrogenase [Chemical/Ingredient], Reduced ferredoxin:dinitrogen oxidoreductase (ATP-hydrolysing) 
An enzyme system that catalyzes the fixing of nitrogen in soil bacteria and blue-green algae (CYANOBACTERIA). EC 1.18.6.1.
National Institutes of Health

Papers overview

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Review
2014
Review
2014
Brian M. Hoffman,* Dmitriy Lukoyanov, Zhi-Yong Yang,† Dennis R. Dean,*,‡ and Lance C. Seefeldt*,† †Department of Chemistry and… Expand
Highly Cited
2011
Highly Cited
2011
A central light atom in a cofactor at the nitrogenase active site is identified as a carbon. Nitrogenase is a complex enzyme that… Expand
Review
2009
Review
2009
Nitrogen-fixing bacteria catalyze the reduction of dinitrogen (N(2)) to two ammonia molecules (NH(3)), the major contribution of… Expand
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Review
2003
Review
2003
Biological nitrogen fixation is an important source of fixed nitrogen for the biosphere. Microorganisms catalyse biological… Expand
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Highly Cited
2002
Highly Cited
2002
A high-resolution crystallographic analysis of the nitrogenase MoFe-protein reveals a previously unrecognized ligand coordinated… Expand
Highly Cited
1992
Highly Cited
1992
Structural models for the nitrogenase FeMo-cofactor and P-clusters are proposed based on crystallographic analysis of the… Expand
Highly Cited
1992
Highly Cited
1992
The nitrogenase enzyme system catalyzes the ATP (adenosine triphosphate)-dependent reduction of dinitrogen to ammonia during the… Expand
Highly Cited
1992
Highly Cited
1992
The crystal structure of the nitrogenase molybdenum–iron protein from Azotobacter vinelandii has been determined at 2.7… Expand
Highly Cited
1986
Highly Cited
1986
The requirement for molybdenum in biological dinitrogen fixation, first reported by Bortels1, is due to its involvement at or… Expand
Highly Cited
1977
Highly Cited
1977
  • V. K. Shah, W. Brill
  • Proceedings of the National Academy of Sciences…
  • 1977
  • Corpus ID: 37440084
A method for the isolation of an iron-molybdenum cofactor (FeMoCo) from component I of nitrogenase is described. This method is… Expand