Reactivity of the Excited States of the H-Cluster of FeFe Hydrogenases

Sensi, Matteo, Baffert, Carole, Greco, Claudio , Caserta, Giorgio, Gauquelin, Charles, Saujet, Laure, Fontecave, Marc, Roy, Souvik, Artero, Vincent, Soucaille, Philippe, Meynial-Salles, Isabelle, Bottin, Hervé, de Gioia, Luca, Fourmond, Vincent, Léger, Christophe and Bertini, Luca (2016) Reactivity of the Excited States of the H-Cluster of FeFe Hydrogenases. Journal of the American Chemical Society, 138 (41). pp. 13612-13618. ISSN 0002-7863

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FeFe hydrogenases catalyze H2 oxidation and formation at an inorganic active site (the “H-cluster”), which consists of a [Fe2(CO)3(CN)2(dithiomethylamine)] subcluster covalently attached to a Fe4S4 subcluster. This active site is photosensitive: visible light has been shown to induce the release of exogenous CO (a reversible inhibitor of the enzyme), shuffle the intrinsic CO ligands, and even destroy the H-cluster. These reactions must be understood because they may negatively impact the use of hydrogenase for the photoproduction of H2. Here, we explore in great detail the reactivity of the excited states of the H-cluster under catalytic conditions by examining, both experimentally and using TDDFT calculations, the simplest photochemical reaction: the binding and release of exogenous CO. A simple dyad model can be used to predict which excitations are active. This strategy could be used for probing other aspects of the photoreactivity of the H-cluster.

Keywords:Dissociation, Peptides and proteins, Energy, Excited states, Irradiation
Subjects:C Biological Sciences > C720 Biological Chemistry
F Physical Sciences > F100 Chemistry
F Physical Sciences > F161 Organometallic Chemistry
Divisions:College of Science > School of Chemistry
ID Code:40675
Deposited On:17 Apr 2020 09:19

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