Recent advances aimed at modeling the chemistry of the active site of [FeFe]-hydrogenases (the H-cluster, composed by a catalytic Fe 2S 2 subcluster and an Fe 4S 4 portion) have led to the synthesis of binuclear coordination compounds containing a noninnocent organophosphine ligand [2,3-bis(diphenylphosphino)maleic anhydride, bma] that is able to undergo monoelectron reduction, analogously to the tetranuclear Fe 4S 4 subcluster portion of the H-cluster. However, such a synthetic model was shown to feature negligible electronic communication between the noninnocent ligand and the remaining portion of the cluster, at variance with the enzyme active site. Here, we report a theoretical investigation that shows why the electron transfer observed in the enzyme upon protonation of the catalytic Fe 2S 2 subsite cannot take place in the bma-containing cluster. In addition, we show that targeted modifications of the bma ligand are sufficient to restore the electronic communication within the model, such that electron density can be more easily withdrawn from the noninnocent ligand, as a result of protonation of the iron centers. Similar results were also obtained with a ligand derived from cobaltocene. The relevance of our findings is discussed from the perspective of biomimetic reproduction of proton reduction to yield molecular hydrogen. © 2011 American Chemical Society.

Greco, C., DE GIOIA, L. (2011). A Theoretical Study on the Enhancement of Functionally Relevant Electron Transfers in Biomimetic Models of [FeFe]-Hydrogenases. INORGANIC CHEMISTRY, 50(15), 6987-6995 [10.1021/ic200297d].

A Theoretical Study on the Enhancement of Functionally Relevant Electron Transfers in Biomimetic Models of [FeFe]-Hydrogenases

GRECO, CLAUDIO;DE GIOIA, LUCA
2011

Abstract

Recent advances aimed at modeling the chemistry of the active site of [FeFe]-hydrogenases (the H-cluster, composed by a catalytic Fe 2S 2 subcluster and an Fe 4S 4 portion) have led to the synthesis of binuclear coordination compounds containing a noninnocent organophosphine ligand [2,3-bis(diphenylphosphino)maleic anhydride, bma] that is able to undergo monoelectron reduction, analogously to the tetranuclear Fe 4S 4 subcluster portion of the H-cluster. However, such a synthetic model was shown to feature negligible electronic communication between the noninnocent ligand and the remaining portion of the cluster, at variance with the enzyme active site. Here, we report a theoretical investigation that shows why the electron transfer observed in the enzyme upon protonation of the catalytic Fe 2S 2 subsite cannot take place in the bma-containing cluster. In addition, we show that targeted modifications of the bma ligand are sufficient to restore the electronic communication within the model, such that electron density can be more easily withdrawn from the noninnocent ligand, as a result of protonation of the iron centers. Similar results were also obtained with a ligand derived from cobaltocene. The relevance of our findings is discussed from the perspective of biomimetic reproduction of proton reduction to yield molecular hydrogen. © 2011 American Chemical Society.
Articolo in rivista - Articolo scientifico
hydrogen
English
2011
50
15
6987
6995
none
Greco, C., DE GIOIA, L. (2011). A Theoretical Study on the Enhancement of Functionally Relevant Electron Transfers in Biomimetic Models of [FeFe]-Hydrogenases. INORGANIC CHEMISTRY, 50(15), 6987-6995 [10.1021/ic200297d].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/45958
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