Nitrogenase: standing at the crossroads

Nitrogenase 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, biochemic...

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Bibliographic Details
Published in:Current Opinion in Chemical Biology 2000-10, Vol.4 (5), p.559-566
Main Authors: Rees, Douglas C, Howard, James B
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - metabolism
Catalysis
Enzyme mechanism
EPR
FE protein
Kinetics
Metalloclusters
MoFe protein
Nitrogenase
Nitrogenase - metabolism
Oxidation-Reduction
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Summary:Nitrogenase 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 approaches to a challenging problem with implications for a range of biochemical and chemical systems.
ISSN:1367-5931
1879-0402
DOI:10.1016/S1367-5931(00)00132-0