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Curr Opin Chem Biol. 2000 Oct;4(5):559-66.

Nitrogenase: standing at the crossroads.

Author information

1
Howard Hughes Medical Institute, Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125, USA. dcrees@caltech.edu

Abstract

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.

PMID:
11006545
DOI:
10.1016/s1367-5931(00)00132-0
[Indexed for MEDLINE]

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