Triiron clusters derived from dinuclear complexes related to the active site of [Fe–Fe] hydrogenases: steric effect of the dithiolate bridge on redox properties, a DFT analysis

Author:

Hobballah Ahmad1234,Arrigoni Federica5678ORCID,Elleouet Catherine1234,Greco Claudio98ORCID,Laurans Maxime1234,Pétillon François Y.1234,Schollhammer Philippe1234ORCID

Affiliation:

1. UMR CNRS 6521

2. Université de Bretagne Occidentale

3. Brest

4. France

5. Department of Biotechnology and Biosciences

6. University of Milan-Bicocca

7. 20126 Milan

8. Italy

9. Department of Earth and Environmental Sciences University of Milan-Bicocca

Abstract

CV and DFT calculations reveal that electrochemical behaviours of triiron clusters [Fe3(CO)52-dppe)(μ-pdtR2)(μ-pdt)] depend on the nature of the dithiolate bridge.

Funder

Centre National de la Recherche Scientifique

Université de Bretagne Occidentale

Università degli Studi di Milano-Bicocca

Région Bretagne

Publisher

Royal Society of Chemistry (RSC)

Subject

Inorganic Chemistry

Reference79 articles.

1. X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom Resolution

2. Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center

3. Biomimetic assembly and activation of [FeFe]-hydrogenases

4. Bioinspired Catalysis: Metal-Sulfur Complexes , ed. W. Weigand , P. Schollhammer , Wiley-VCH-Verl , Weinheim , 2015 , pp. 417

5. C. Elleouet , F. Y.Pétillon and P.Schollhammer , in Advances in bioorganometallic chemistry : [FeFe]-hydrogenases Models , ed. T. Hirao and T. Moriuchi , Elsevier , 2019 , ch. 17, pp. 347–359

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