Abstract
The reduction of dinitrogen (N2) to ammonia (NH3) by nitrogenase MoFe protein is coupled to chemically driven electron transfer by nitrogenase Fe protein, where H2 is an obligatory side product. Direct coupling of light-absorbing semiconductor nanocrystals to MoFe protein enables NH3 production from photoexcited electron transfer, replacing Fe protein. Production of H2 and NH3 was measured for CdS quantum dot (QD) MoFe protein complexes illuminated under different excitation rates. 15N-labeling of NH3 production combined with background-corrected H2 production enabled determination of MoFe protein catalysis products. The turnover rates of H2 and NH3 increased with excitation rate, with distinct kinetic responses that show the electron demand for NH3 requires higher excitation rates to overcome the more favored H2 production.
Original language | American English |
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Pages (from-to) | 11147-11152 |
Number of pages | 6 |
Journal | ACS Catalysis |
Volume | 10 |
Issue number | 19 |
DOIs | |
State | Published - 2 Oct 2020 |
Bibliographical note
Publisher Copyright:Copyright © 2020 American Chemical Society.
NREL Publication Number
- NREL/JA-2700-77389
Keywords
- 15N2
- ammonia
- biohybrid
- CdS quantum dot
- nitrogenase
- photoexcitation rate
- solar fuels