reviewAnnual Review of BiochemistryJun 1, 2009GREEN OA

Mechanism of Mo-Dependent Nitrogenase

Utah State University · Northwestern University · +1 more institution

PubMed
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Abstract

Nitrogen-fixing bacteria catalyze the reduction of dinitrogen (N(2)) to two ammonia molecules (NH(3)), the major contribution of fixed nitrogen to the biogeochemical nitrogen cycle. The most widely studied nitrogenase is the molybdenum (Mo)-dependent enzyme. The reduction of N(2) by this enzyme involves the transient interaction of two component proteins, designated the iron (Fe) protein and the MoFe protein, and minimally requires 16 magnesium ATP (MgATP), eight protons, and eight electrons. The current state of knowledge on how these proteins and small molecules together effect the reduction of N(2) to ammonia is reviewed. Included is a summary of the roles of the Fe protein and MgATP hydrolysis, information…

Citation impact

667
total citations
FWCI
18.82
Percentile
100%
References
178
Citations per year

Authors

3

Topics & keywords

Keywords
  • Nitrogenase
  • Chemistry
  • Cofactor
  • Enzyme
  • Nitrogen fixation
  • Molybdenum
  • Catalysis
  • Metal
UN Sustainable Development Goals
  • Clean water and sanitation
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