A sterically stabilized FeI–FeI semi-rotated conformation of [FeFe] hydrogenase subsite model-Reference-Cited by-同舟云学术

A sterically stabilized FeI–FeI semi-rotated conformation of [FeFe] hydrogenase subsite model

Published:2015 Issue:4 Volume:44 Page:1690-1699
ISSN:1477-9226
Container-title:Dalton Transactions
language:en
Short-container-title:Dalton Trans.

Author:

Goy Roman¹²³⁴,Bertini Luca⁵⁶⁷,Elleouet Catherine⁸⁹¹⁰¹¹¹²,Görls Helmar¹²³⁴,Zampella Giuseppe⁵⁶⁷,Talarmin Jean⁸⁹¹⁰¹¹¹²,De Gioia Luca⁵⁶⁷,Schollhammer Philippe⁸⁹¹⁰¹¹¹²,Apfel Ulf-Peter¹³¹⁴¹⁵⁴,Weigand Wolfgang¹²³⁴¹⁶

Affiliation:

1. Institut für Anorganische und Analytische Chemie

2. Friedrich-Schiller-Universität

3. 07743 Jena

4. Germany

5. Department of Biotechnology and Biosciences

6. University of Milano-Bicocca

7. Italy

8. University of Brest

9. CNRS

10. UMR 6521

11. Chimie

12. Electrochimie Moléculaires et Chimie Analytique

13. Inorganic Chemistry I/Bioinorganic Chemistry

14. Ruhr-Universität Bochum

15. 44780 Bochum

16. Jena Center for Soft Matter (JCSM)

Abstract

Semi-rotated state – As the first example so far a [Fe^IFe^I] H₂ase model complex with a bulky silicon-containing dithiolate bridge is reported showing a semi-rotated geometry without the need of stabilization via agostic interactions.

Publisher

Royal Society of Chemistry (RSC)

Subject

Inorganic Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2015/DT/C4DT03223C

Reference68 articles.

1. Catalytic Turnover of [FeFe]-Hydrogenase Based on Single-Molecule Imaging

2. Chemistry and the hydrogenases

3. Structure–function relationships of nickel–iron sites in hydrogenase and a comparison with the active sites of other nickel–iron enzymes

4. A Mixed-Valent, Fe(II)Fe(I), Diiron Complex Reproduces the Unique Rotated State of the [FeFe]Hydrogenase Active Site

5. Synthetic Support of De Novo Design: Sterically Bulky [FeFe]-Hydrogenase Models

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