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Cited by 232

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

How many metals does it take to fix N 2 ? A mechanistic overview of biological nitrogen fixation

Open access
Howard, James B., Rees, Douglas C.·2006·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.0603978103
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Abstract

During the process of biological nitrogen fixation, the enzyme nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia. Nitrogenase consists of two component metalloproteins, the iron (Fe) protein and the molybdenum-iron (MoFe) protein; the Fe protein mediates the coupling of ATP hydrolysis to interprotein electron transfer, whereas the active site of the MoFe protein contains the polynuclear FeMo cofactor, a species composed of seven iron atoms, one molybdenum atom, nine sulfur atoms, an interstitial light atom, and one homocitrate molecule. This Perspective provides an overview of biological nitrogen fixation and introduces three contributions to this special feature that address central aspects of the mechanism and assembly of nitrogenase.

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Cited by

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Metadata

Authors
Howard, J. B., & Rees, D. C.
Venue
Proceedings of the National Academy of Sciences
Publisher
Proceedings of the National Academy of Sciences
Published
2006-11-14
Volume
103
Issue
46
Pages
17088-17093
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.0603978103
OpenAlex
W2039568374
Cited by
232
References
3
FWCI
10.49
Type
journal article
Language
en
Open access
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CoChat. (2026). Citation check: How many metals does it take to fix N 2 ? A mechanistic overview of biological nitrogen fixation. https://app.cochat.ai/papers/10.1073/pnas.0603978103
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Howard, J. B., & Rees, D. C. (2006). How many metals does it take to fix N 2 ? A mechanistic overview of biological nitrogen fixation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0603978103

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