On the electrochemistry of diiron dithiolate complexes related to the active site of the [FeFe]H2ase
Author:
Publisher
Elsevier BV
Subject
General Chemical Engineering,General Chemistry
Reference76 articles.
1. X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom Resolution
2. Binding of Exogenously Added Carbon Monoxide at the Active Site of the Iron-Only Hydrogenase (CpI) from Clostridium pasteurianum,
3. Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center
4. Crystallographic and FTIR Spectroscopic Evidence of Changes in Fe Coordination Upon Reduction of the Active Site of the Fe-Only Hydrogenase from Desulfovibrio desulfuricans
5. Carbon Monoxide and Cyanide Ligands in a Classical Organometallic Complex Model for Fe-Only Hydrogenase
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1. Mechanism of Diiron Hydrogenase Complexes Controlled by Nature of Bridging Dithiolate Ligand;ChemistryOpen;2022-01
2. [FeFe]-Hydrogenases: maturation and reactivity of enzymatic systems and overview of biomimetic models;Chemical Society Reviews;2021
3. Iron carbonyl compounds with aromatic dithiolate bridges as organometallic mimics of [FeFe] hydrogenases;Coordination Chemistry Reviews;2020-01
4. Electronic Communication between Dithiolato-Bridged Diiron Carbonyl and S-Bridged Redox-Active Centres;Inorganics;2019-03-08
5. [FeFe]-Hydrogenases Models;Advances in Bioorganometallic Chemistry;2019
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