2026/06/18 by Malin Khalil, Elizaveta Kobeleva, Cornelius C. M. Bernitzky +9 · 1 voice
Chemistry · Energy · #Electrocatalysts for Energy Conversion #Metal-Catalyzed Oxygenation Mechanisms #Metalloenzymes and iron-sulfur proteins
paper · doi:10.1021/acs.inorgchem.6c01321
openalex publication_date 2026/06/18 · openalex created_date 2026/06/19 · openalex updated_date 2026/08/01
High Resolution Image Download MS PowerPoint Slide Hydrogenases are metalloenzymes that catalyze the reversible splitting of dihydrogen (H 2 ), 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 H 2 binding. Using UV pump -IR probe 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 H 2 binding and activation at the active site, unaffected by H 2 mass transport limitation.