Hydrogen Bonding in the Active Site of Ketosteroid Isomerase: Electronic Inductive Effects and Hydrogen Bond Coupling
Author:
Affiliation:
1. Department of Chemistry, 104 Chemistry Building, Pennsylvania State University, University Park, Pennsylvania 16802, United States
2. Department of Biochemistry, Stanford University, Stanford, California 94305-5080, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi101428e
Reference49 articles.
1. Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase
2. Energetics of 3-oxo-.DELTA.5-steroid isomerase: source of the catalytic power of the enzyme
3. Substituent Effects on the Binding of Phenols to the D38N Mutant of 3-Oxo-Δ5-steroid Isomerase. A Probe for the Nature of Hydrogen Bonding to the Intermediate
4. Testing Electrostatic Complementarity in Enzyme Catalysis: Hydrogen Bonding in the Ketosteroid Isomerase Oxyanion Hole
5. Binding of 2-Naphthols to D38E Mutants of 3-Oxo-Δ5-steroid Isomerase: Variation of Ligand Ionization State with the Nature of the Electrophilic Component
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