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![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
From Carbon-Monoxide Inhibition to Light Activation: Probing [NiFe] Hydrogenase Dynamics by Multiscale Time-Resolved
Malin Khalil1, Elizaveta Kobeleva1, Cornelius C M Bernitzky1
1Department of Physics, Freie Universität Berlin, Ultrafast Dynamics in Catalysis, Arnimallee 14, 14195 Berlin, Germany.
Abstract:
Hydrogenases are metalloenzymes that catalyze the reversible splitting of dihydrogen (H2), a clean and sustainable fuel. In this study, we investigate the reversible photodissociation and rebinding of an extrinsic carbon monoxide (CO) ligand at the active site of a [NiFe] model hydrogenase. CO acts as a catalytic inhibitor of the enzyme, whereas its photolysis restores an active state capable of H2 binding. Using UVpump-IRprobe spectroscopy in a multiple-probe configuration that allows covering picosecond to millisecond time scales, we characterize the reaction dynamics following CO photolysis. The results reveal a large temporal window between rapid CO dissociation and slow rebinding, enabling the detailed investigation of H2 binding and activation at the active site, unaffected by H2 mass transport limitation.
