期刊
CURRENT OPINION IN CHEMICAL BIOLOGY
卷 4, 期 5, 页码 559-566出版社
ELSEVIER SCI LTD
DOI: 10.1016/S1367-5931(00)00132-0
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资金
- NIGMS NIH HHS [GM45162] Funding Source: Medline
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.
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