In this work, we employ density functional theory to assign vibrational signatures of [FeFe]-hydrogenase intermediates to molecular structures. For this purpose, we perform an exhaustive analysis of structures and harmonic vibrations of a series of CN and CO containing model clusters of the [FeFe]-hydrogenase enzyme active site considering also different charges, counterions, and solvents. The pure density functional BP86 in combination with a triple-ζ polarized basis set produce reliable molecular structures as well as harmonic vibrations. Calculated CN and CO stretching vibrations are analyzed separately. Scaled vibrational frequencies are then applied to assign intermediates in [FeFe]-hydrogenase's reaction cycle. The results nicely complement the previous studies of Darensbourg and Hall,(1),(2)and Zilberman et al.(3)-(5)The infrared spectrum of the Hox form is in very good agreement with the calculated spectrum of the Fe IFeII model complex featuring a free coordination site at the distal Fe atom, as well as, with the calculated spectra of the complexes in which H2 or H2O are coordinated at this site. The spectrum of Hred measured from Desulfovibrio desulfuricans is compatible with a mixture of a FeIFeI species with all terminal COs, and a FeIFeI species with protonated dtma ligand, while the spectrum of Hred recently measured from Chlamydomonas reinhardtii is compatible with a mixture of a FeIFeI species with a bridged CO, and a FeIIFeII species with a terminal hydride bound to the Fe atom. © 2011 American Chemical Society.

Yu, L., Greco, C., Bruschi, M., Ryde, U., DE GIOIA, L., Reiher, M. (2011). Targeting Intermediates of [FeFe]-Hydrogenase by CO and CN Vibrational Signatures. INORGANIC CHEMISTRY, 50(9), 3888-3900 [10.1021/ic102039z].

Targeting Intermediates of [FeFe]-Hydrogenase by CO and CN Vibrational Signatures

GRECO, CLAUDIO;BRUSCHI, MAURIZIO;DE GIOIA, LUCA;
2011

Abstract

In this work, we employ density functional theory to assign vibrational signatures of [FeFe]-hydrogenase intermediates to molecular structures. For this purpose, we perform an exhaustive analysis of structures and harmonic vibrations of a series of CN and CO containing model clusters of the [FeFe]-hydrogenase enzyme active site considering also different charges, counterions, and solvents. The pure density functional BP86 in combination with a triple-ζ polarized basis set produce reliable molecular structures as well as harmonic vibrations. Calculated CN and CO stretching vibrations are analyzed separately. Scaled vibrational frequencies are then applied to assign intermediates in [FeFe]-hydrogenase's reaction cycle. The results nicely complement the previous studies of Darensbourg and Hall,(1),(2)and Zilberman et al.(3)-(5)The infrared spectrum of the Hox form is in very good agreement with the calculated spectrum of the Fe IFeII model complex featuring a free coordination site at the distal Fe atom, as well as, with the calculated spectra of the complexes in which H2 or H2O are coordinated at this site. The spectrum of Hred measured from Desulfovibrio desulfuricans is compatible with a mixture of a FeIFeI species with all terminal COs, and a FeIFeI species with protonated dtma ligand, while the spectrum of Hred recently measured from Chlamydomonas reinhardtii is compatible with a mixture of a FeIFeI species with a bridged CO, and a FeIIFeII species with a terminal hydride bound to the Fe atom. © 2011 American Chemical Society.
Articolo in rivista - Articolo scientifico
FE-ONLY HYDROGENASES; DENSITY-FUNCTIONAL THEORY; QUANTUM-CHEMICAL CALCULATION; TRANSITION-METAL DIMERS; IRON-SULFUR CLUSTERS; ACTIVE-SITE; H-CLUSTER; DESULFOVIBRIO-DESULFURICANS; ELECTRONIC-STRUCTURE; CLOSTRIDIUM-PASTEURIANUM
English
2011
50
9
3888
3900
none
Yu, L., Greco, C., Bruschi, M., Ryde, U., DE GIOIA, L., Reiher, M. (2011). Targeting Intermediates of [FeFe]-Hydrogenase by CO and CN Vibrational Signatures. INORGANIC CHEMISTRY, 50(9), 3888-3900 [10.1021/ic102039z].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/28606
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