Moessbauer studies of model complexes for the H-cluster in [Fe-Fe]-hydrogenases: Electronic structure of mixed-valence complexes containing low-spin Fe(I)

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Title:	Moessbauer studies of model complexes for the H-cluster in [Fe-Fe]-hydrogenases: Electronic structure of mixed-valence complexes containing low-spin Fe(I)
Authors:	Popescu, Codrina V.;Stoian, Sebastian A.;Hsieh, Chung-Hung;Darensbourg, Marcetta Y.;Casuras, Andrea
Contributors:	淡江大學化學學系
Date:	2012-08
Issue Date:	2014-03-28
Abstract:	Hydrogenases are enzymes that catalyze the reversible conversion of protons to mol. hydrogen. The active site of the [Fe-Fe]-hydrogenases (the H-cluster) can provide the required potential for this reaction using iron in low oxidn. states. Since it has been recognized that the H-cluster may contain low-spin Fe(I), monovalent iron has become a focus of bio-organometallic synthetic chem. In spite of its intriguing implication in hydrogenogenesis, the electronic structure of low-spin Fe(I) is unknown. The high asymmetry of the dinuclear site in the H-cluster stabilizes the elusive Fe(I)Fe(II...
Relation:	244th ACS National Meeting & Exposition, INOR-699
Appears in Collections:	[Graduate Institute & Department of Chemistry] Proceeding

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