Probing the Effects of One-Electron Reduction and Protonation on the Electronic Properties of the Fe-S Clusters in the Active-Ready Form of [FeFe]-Hydrogenases. A QM/MM Investigation.
Author:
Publisher
Wiley
Subject
Physical and Theoretical Chemistry,Atomic and Molecular Physics, and Optics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/cphc.201100498/fullpdf
Reference52 articles.
1. Crystallographic and FTIR Spectroscopic Evidence of Changes in Fe Coordination Upon Reduction of the Active Site of the Fe-Only Hydrogenase from Desulfovibrio desulfuricans
2. X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom Resolution
3. Binding of Exogenously Added Carbon Monoxide at the Active Site of the Iron-Only Hydrogenase (CpI) from Clostridium pasteurianum,
4. 14N HYSCORE investigation of the H-cluster of [FeFe] hydrogenase: evidence for a nitrogen in the dithiol bridge
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4. Proton Coupled Electronic Rearrangement within the H-Cluster as an Essential Step in the Catalytic Cycle of [FeFe] Hydrogenases;Journal of the American Chemical Society;2017-01-17
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