Advanced Electron Paramagnetic Resonance and Density Functional Theory Study of a {2Fe3S} Cluster Mimicking the Active Site of [FeFe] Hydrogenase
Author:
Affiliation:
1. Max-Planck-Institut für Bioanorganische Chemie, Stiftstrasse 34-36, Mülheim an der Ruhr, 45470, Germany
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja107793e
Reference58 articles.
1. [NiFe] and [FeFe] Hydrogenases Studied by Advanced Magnetic Resonance Techniques
2. Crystallographic and FTIR Spectroscopic Evidence of Changes in Fe Coordination Upon Reduction of the Active Site of the Fe-Only Hydrogenase from Desulfovibrio desulfuricans
3. X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom Resolution
4. The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. I. Light sensitivity and magnetic hyperfine interactions as observed by electron paramagnetic resonance
5. The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. II. Redox properties, light sensitivity and CO-ligand exchange as observed by infrared spectroscopy
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