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vanadium-iron nitrogenase complex

Known as: vanadium-iron nitrogenase complex location 
An enzyme complex containing a vanadium-iron cluster found in some species, such as Azotobacter vinelandii. It is composed of two proteins… Expand
National Institutes of Health

Papers overview

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2017
2017
Nitrogenase is the only known biological system capable of reducing N2 to NH3 , which is a critical component of bioavailable… Expand
Highly Cited
2016
Highly Cited
2016
Nitrogenase is the only enzyme known to catalyze the reduction of N2 to 2NH3. In vivo, the MoFe protein component of nitrogenase… Expand
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Review
2012
Review
2012
  • J. Raven
  • Plant science : an international journal of…
  • 2012
  • Corpus ID: 22209540
Phosphorus (P) is the proximate (immediate) limiting element for primary productivity in some habitats, and is generally the… Expand
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2011
2011
Iron is widely thought to limit nitrogen fixation in the open, oligotrophic ocean due to the low solubility of Fe in oxic… Expand
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2007
2007
The heterocyst is a specialized cell for nitrogen fixation in some filamentous cyanobacteria. Here we report that a rubrerythrin… Expand
Highly Cited
2006
Highly Cited
2006
Nitrogenase catalyzes a reaction critical for life, the reduction of N(2) to 2NH(3), yet we still know relatively little about… Expand
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Highly Cited
2004
Highly Cited
2004
Ammonium salts, glutamine, asparagine, and urea cause an immediate inactivation (switch-off) of light-dependent acetylene… Expand
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1991
1991
Azotobacter vinelandii DJ71, which contains a mutation in the nifV gene, was derepressed for nitrogenase in the presence of… Expand
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1986
1986
  • M. Drummond
  • European journal of biochemistry
  • 1986
  • Corpus ID: 19995885
A first approximation to the tertiary structure of the nitrogenase flavodoxins of Klebsiella pneumoniae and Azotobacter… Expand
1978
1978
  • D. Werner
  • Zeitschrift fur Naturforschung. Section C…
  • 1978
  • Corpus ID: 19614063
Development of nitrogenase (40 -140 nmol C2 H4 · mg protein-1· h-1) in Rhizobium japonicum 61-A-101 after transfer to special… Expand
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