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Title: Light-Driven Dinitrogen Reduction Catalyzed by a CdS: Nitrogenase MoFe Protein Biohybrid

The splitting of dinitrogen (N2) and reduction to ammonia (NH3) is a kinetically complex and energetically challenging multistep reaction. In the Haber-Bosch process, N2 reduction is accomplished at high temperature and pressure, whereas N2 fixation by the enzyme nitrogenase occurs under ambient conditions using chemical energy from adenosine 5'-triphosphate (ATP) hydrolysis. We show that cadmium sulfide (CdS) nanocrystals can be used to photosensitize the nitrogenase molybdenum-iron (MoFe) protein, where light harvesting replaces ATP hydrolysis to drive the enzymatic reduction of N2 into NH3. The turnover rate was 75 per minute, 63% of the ATP-coupled reaction rate for the nitrogenase complex under optimal conditions. Inhibitors of nitrogenase (i.e., acetylene, carbon monoxide, and dihydrogen) suppressed N2 reduction. The CdS:MoFe protein biohybrids provide a photochemical model for achieving light-driven N2 reduction to NH3.
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Publication Date:
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Resource Type:
Journal Article
Resource Relation:
Journal Name: Science; Journal Volume: 352; Journal Issue: 6284; Related Information: Science
Research Org:
NREL (National Renewable Energy Laboratory (NREL), Golden, CO (United States))
Sponsoring Org:
USDOE Office of Science (SC); NREL Laboratory Directed Research and Development (LDRD)
Country of Publication:
United States
09 BIOMASS FUELS; 37 INORGANIC, ORGANIC, PHYSICAL, AND ANAYLYTICAL CHEMISTRY CdS nanorod:MoFe protein complex; photocatalyze; reduction of N2 into NH3