A Model of the [FeFe] Hydrogenase Active Site with a Biologically Relevant Azadithiolate Bridge: A Spectroscopic and Theoretical Investigation-Reference-Cited by-同舟云学术

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A Model of the [FeFe] Hydrogenase Active Site with a Biologically Relevant Azadithiolate Bridge: A Spectroscopic and Theoretical Investigation

Published:2011-01-05 Issue:6 Volume:50 Page:1439-1443
ISSN:1433-7851
Container-title:Angewandte Chemie International Edition
language:en
Short-container-title:Angew. Chem. Int. Ed.

Author:

Erdem Özlen F.,Schwartz Lennart,Stein Matthias,Silakov Alexey,Kaur-Ghumaan Sandeep,Huang Ping,Ott Sascha,Reijerse Edward J.,Lubitz Wolfgang

Publisher

Wiley

Subject

General Chemistry,Catalysis

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/anie.201006244/fullpdf

Reference51 articles.

1. A novel FeS cluster in Fe-only hydrogenases

2. Structure–function relationships of anaerobic gas-processing metalloenzymes

3. Crystallographic and FTIR Spectroscopic Evidence of Changes in Fe Coordination Upon Reduction of the Active Site of the Fe-Only Hydrogenase from Desulfovibrio desulfuricans

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

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2. Facile electrocatalytic proton reduction by a [Fe–Fe]-hydrogenase bio-inspired synthetic model bearing a terminal CN⁻ ligand;Chemical Science;2024

3. Photophysics of Fe-Fe hydrogenase mimic complexes for hydrogen evolution;Journal of Organometallic Chemistry;2024-01

4. Molecular Catalysis of Energy Relevance in Metal–Organic Frameworks: From Higher Coordination Sphere to System Effects;Chemical Reviews;2023-05-15

5. [FeFe]‐Hydrogenase models featuring dithiolato‐bridgehead functionality: Preparation, structures, and electrocatalytic proton reduction;Zeitschrift für anorganische und allgemeine Chemie;2022-11-24

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