Coordination Sphere Flexibility of Active-Site Models for Fe-Only Hydrogenase: Studies in Intra- and Intermolecular Diatomic Ligand Exchange
Author:
Affiliation:
1. Contribution from the Department of Chemistry, Texas A&M University, College Station, Texas 77843
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja003147z
Reference63 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. A novel FeS cluster in Fe-only hydrogenases
5. Biological activition of hydrogen
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