Direct Evidence of Active-Site Reduction and Photodriven Catalysis in Sensitized Hydrogenase Assemblies

What is it about?

This article describes a abiotic-biotic chimera assembly of CdTe quantum dots electrostatically bound to a [NiFe]-Hydrogenase for light driven hydrogen production. This work expanded on earlier studies from the group of Dr. Paul King, which utilized a [FeFe]-Hydrogenase in a similar mechanism to drive proton reduction with visible light, but advanced the technology using a more oxygen stable Hydrogenase and in situ infrared spectroscopy for enzyme characterization.

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Why is it important?

The import of this work is two fold: (1) using energy derived from light to drive proton reduction represents a potentially renewable source of energy which can be stored indefinitely as opposed to purely photo-voltaic technologies, and (2) using light to gate proton reduction in the QD-Hydrogenase assembly represents a novel method for mechanistically interrogating the hydrogenase enzyme which operates at extremely rapid rates ( > 1,000 molecules hydrogen per second per enzyme).