How many metals does it take to fix N2? A mechanistic overview of biological nitrogen fixation
- Creators
- Howard, James B.
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Rees, Douglas C.
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.
Additional Information
© 2006 by the National Academy of Sciences. Edited by Richard R. Schrock, Massachusetts Institute of Technology, Cambridge, MA, and approved June 28, 2006 (received for review May 19, 2006). Published online on November 6, 2006, 10.1073/pnas.0603978103. We thank members of the Howard and Rees groups, past, present, and future, for their contributions to the nitrogenase project in our laboratories. This work was supported in part by National Institutes of Health Grant GM045162.Attached Files
Published - HOWpnas06.pdf
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Additional details
- PMCID
- PMC1859894
- Eprint ID
- 9607
- Resolver ID
- CaltechAUTHORS:HOWpnas06
- Created
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2008-02-18Created from EPrint's datestamp field
- Updated
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2021-11-08Created from EPrint's last_modified field