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Inside Cover, Volume 114, Issue 13
Publication year - 2014
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.24702
Subject(s) - cover (algebra) , hydrogenase , adduct , chemistry , hydrogen , volume (thermodynamics) , solvent , computer science , photochemistry , physics , thermodynamics , organic chemistry , engineering , mechanical engineering
[FeFe] hydrogenase enzymes efficiently and reversibly catalyze the reduction of protons to molecular hydrogen. Biomimetic active site models can also photocatalyze the formation of hydrogen, though with low yields. To improve the efficiency of hydrogen photoproduction, it is crucial to understand the photochemistry of the models in detail. For this reason, the photochemistry of Fe 2 (S 2 C 3 H 6 )(CO) 6 , using a simple [FeFe] hydrogenase model, is investigated at an experimental level. Upon irradiation, this model undergoes CO photolysis to form a solvent adduct. On page 851 (DOI: 10.1002/qua.24667 ), Luca Bertini, Claudio Greco, Piercarlo Fantucci, and Luca De Gioia detail this photochemical process at DFT and TDDFT levels.