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Cited by 444

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Nitrogenase and biological nitrogen fixation

Kim, Jongsun, Rees, Douglas C.·1994·Biochemistry

Abstract

Biological nitrogen fixation is catalyzed by the nitrogenase enzyme system which consists of two metalloproteins, the iron (Fe-) protein and the molybdenum-iron (MoFe-) protein. Together, these proteins mediate the ATP-dependent reduction of dinitrogen to ammonia. Recent crystallographic analyses of Fe-protein and MoFe-protein have revealed the polypeptide fold and the structure and organization of the unusual metal centers in nitrogenase. These structure provide a molecular framework for addressing the mechanism of the nitrogenase-catalyzed reaction. General features of the nitrogenase system, including conformational coupling of nucleotide hydrolysis, aspects of the cluster structures, and the general spatial organization of redox centers within the protein subunits, are relevant to a wide range of biochemical systems.

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Metadata

Authors
Kim, J., & Rees, D. C.
Venue
Biochemistry
Published
1994-01-18
Volume
33
Issue
2
Pages
389-397
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
OpenAlex
W2002564429
Cited by
444
References
1
FWCI
28.37
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Nitrogenase and biological nitrogen fixation. https://app.cochat.ai/papers/10.1021/bi00168a001
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Kim, J., & Rees, D. C. (1994). Nitrogenase and biological nitrogen fixation. Biochemistry. https://doi.org/10.1021/bi00168a001

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