Published October 2000
| public
Journal Article
Nitrogenase: Standing at the Crossroads
- Creators
-
Rees, Douglas C.
- Howard, James B.
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.
Additional Information
© 2000 Elsevier Science Ltd. Discussions with members of our groups and nitrogenase colleagues are greatly appreciated. Research in the authors' laboratory was supported by United States Public Health Service grant GM45162 (DCR and JBH) and National Science Foundation MCB9513512 (JBH).Additional details
- Eprint ID
- 53412
- Resolver ID
- CaltechAUTHORS:20150108-154309553
- GM45162
- USPHS
- MCB9513512
- NSF
- Created
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2015-01-14Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field