Light-driven dinitrogen reduction catalyzed by a CdS:nitrogenase MoFe protein biohybrid

Katherine A. Brown, Derek F. Harris, Molly B. Wilker, Andrew Rasmussen, Nimesh Khadka, Hayden Hamby, Stephen Keable, Gordana Dukovic, John W. Peters, Lance C. Seefeldt, Paul W. King

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Abstract

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-Œ-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.

Original languageEnglish
Pages (from-to)448-450
Number of pages3
JournalScience
Volume352
Issue number6284
DOIs
StatePublished - Apr 22 2016
Externally publishedYes

Funding

K.A.B. and P.W.K. were supported by a Laboratory Directed Research and Development Program seed project at the National Renewable Energy Laboratory for CdS:MoFe protein photochemical H2 production experiments, and by the U.S. Department of Energy, Office of Basic Energy Sciences, Division of Chemical Sciences, Geosciences, and Biosciences; and the U.S. Department of Energy under Contract no. DE-AC36-08-GO28308 with the National Renewable Energy Laboratory for CdS:MoFe protein biohybrid N2 reduction experiments. M.B.W., H.H., and G.D. conducted .

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