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  • Title: Multiscale modeling of the active site of [Fe] hydrogenase: the H₂ binding site in open and closed protein conformations.
    Author: Hedegård ED, Kongsted J, Ryde U.
    Journal: Angew Chem Int Ed Engl; 2015 May 18; 54(21):6246-50. PubMed ID: 25867218.
    Abstract:
    A series of QM/MM optimizations of the full protein of [Fe] hydrogenase were performed. The FeGP cofactor has been optimized in the water-bound resting state (1), with a side-on bound dihydrogen (2), or as a hydride intermediate (3). For inclusion of H4MPT in the closed structure, advanced multiscale modeling appears to be necessary, especially to obtain reliable distances between CH-H4MPT(+) and the dihydrogen (H2) or hydride (H(-)) ligand in the FeGP cofactor. Inclusion of the full protein is further important for the relative energies of the two intermediates 2 and 3. We finally find that hydride transfer from 3 has a significantly higher barrier than found in previous studies neglecting the full protein environment.
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