Angewandte Chemie International Edition · 1999 · 62 citations · 0 references
Life SciencesBiochemistryChemistryEnzymologyStructural BiochemistryStructural BiologyCatalytic MechanismsHydrogen Bonding In BiomoleculesProtein ChemistryProtein StructureProteolytic EnzymesStructural EnzymologyCatalytic Triad ArchitectureCatalytic Triad MechanismHydrogen BondingHydrogen Bonding In CatalysisHydrogen Bonding ModelsHydrogen Bonds In Enzyme CatalysisNuclear Level DensitiesSerine Protease Mechanism
Low-barrier hydrogen bond (LBHB) involvement in enzyme catalysis is examined by analysis of experimental nuclear and electron densities of a model compound for the catalytic triad in serine proteases (shown schematically), which is based on a cocrystal of betaine, imidazole, and picric acid. The three short, strong N-H⋅⋅⋅O hydrogen bonds in the structure have varying degrees of covalent bonding contributions suggesting a gradual transition to the LBHB situation.