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

Paul King, Katherine Brown, Derek Harris, Molly Wilker, Andrew Rasmussen, Nimesh Khadka, Hayden Hamby, Stephen Keable, Gordana Dukovic, John Peters, Lance Seefeldt

Research output: Contribution to journalArticlepeer-review

680 Scopus Citations


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 languageAmerican English
Pages (from-to)448-450
Number of pages3
Issue number6284
StatePublished - 22 Apr 2016

NREL Publication Number

  • NREL/JA-2700-65820


  • CdS nanorod:MoFe protein complex
  • photocatalyze
  • reduction of N2 into NH3


Dive into the research topics of 'Light-Driven Dinitrogen Reduction Catalyzed by a CdS: Nitrogenase MoFe Protein Biohybrid'. Together they form a unique fingerprint.

Cite this