Characterization of the active site of catalytically inactive forms of [NiFe] hydrogenases by density functional theory.
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The inactive forms, unready (Ni-A, Ni-SU) and ready (Ni-B), of NiFe hydrogenases are modeled by examining the possibility of hydroxo, oxo, hydroperoxo, peroxo, and sulfenate groups in active-site models and comparing predicted IR frequencies and g tensors with those of the enzyme. The best models for Ni-A and Ni-SU have hydroxo (mu-OH) bridges between Fe and Ni and a terminal sulfenate [Ni-S(=O)Cys] group, although a hydroperoxo model for Ni-A is also quite viable, whereas the best model for Ni-B has only a mu-OH bridge. In addition, a mechanism for the activation of unready hydrogenase is proposed on the basis of the relative stabilities of sulfenate models versus peroxide models.
author list (cited authors)
Pardo, A., De Lacey, A. L., Fernndez, V. M., Fan, Y., & Hall, M. B.
complete list of authors
Pardo, Alejandro||De Lacey, Antonio L||Fernández, Víctor M||Fan, Yubo||Hall, Michael B