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Nitrogenase: Standing at the Crossroads

Rees, Douglas C. and Howard, James B. (2000) Nitrogenase: Standing at the Crossroads. Current Opinion in Chemical Biology, 4 (5). pp. 559-566. ISSN 1367-5931. doi:10.1016/S1367-5931(00)00132-0.

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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.

Item Type:Article
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URLURL TypeDescription DOIArticle
Rees, Douglas C.0000-0003-4073-1185
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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).
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Subject Keywords:Nitrogenase; EPR; Metalloclusters; FE protein; MoFe protein; Enzyme mechanism
Issue or Number:5
Record Number:CaltechAUTHORS:20150108-154309553
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Official Citation:Douglas C Rees, James B Howard, Nitrogenase: standing at the crossroads, Current Opinion in Chemical Biology, Volume 4, Issue 5, 1 October 2000, Pages 559-566, ISSN 1367-5931, (
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:53412
Deposited By: SWORD User
Deposited On:14 Jan 2015 07:23
Last Modified:10 Nov 2021 20:01

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