Journal
DALTON TRANSACTIONS
Volume 41, Issue 4, Pages 1118-1127Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c1dt11535a
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Funding
- Herman Frasch Foundation [617-HF07]
- National Institutes of Health [GM 67626]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM067626] Funding Source: NIH RePORTER
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Nitrogenase catalyzes the biological conversion of atmospheric dinitrogen to bioavailable ammonia. The molybdenum (Mo)- and vanadium (V)-dependent nitrogenases are two homologous members of this metalloenzyme family. However, despite their similarities in structure and function, the characterization of V-nitrogenase has taken a much longer and more winding path than that of its Mo-counterpart. From the initial discovery of this nitrogen-fixing system, to the recent finding of its CO-reducing capacity, V-nitrogenase has proven to be a two-hit wonder in the over-a-century-long research of nitrogen fixation. This perspective provides a brief account of the catalytic function and structural basis of V-nitrogenase, as well as a short discussion of the theoretical and practical potentials of this unique metalloenzyme.
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