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PMID: 11006545 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review

Nitrogenase: standing at the crossroads.

Current opinion in chemical biology ·Vol. 4 ·No. 5 ·2000-10-00 ·Pages 559-66

Rees DC, Howard JB

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.

MeSH Terms
Adenosine Triphosphate/metabolism Catalysis Kinetics Nitrogenase/metabolism Oxidation-Reduction
Chemicals
Adenosine Triphosphate Nitrogenase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Rees D C
Howard Hughes Medical Institute, Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125, USA. [email protected]
Howard J B
Article Info
Journal
Current opinion in chemical biology
Abbr.
Curr Opin Chem Biol
ISSN
1367-5931
Published
2000-10-00
Pages
559-66
Language
English
Region
England
NLM ID
9811312
Subset
IM
Grants
NIGMS NIH HHS · GM45162 · United States
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