6533b830fe1ef96bd129727d

RESEARCH PRODUCT

Dependence of enzyme reaction mechanism on protonation state of titratable residues and QM level description: lactate dehydrogenase

Silvia FerrerIan H. WilliamsEstanislao SillaMónica OlivaVicent MolinerIñaki Tuñón

subject

ProtonStereochemistryUNESCO::QUÍMICATitratable acidDehydrogenaseProtonationChemical reactionQM/MM:QUÍMICA [UNESCO]CatalysisSubstrate Specificitychemistry.chemical_compoundComputational chemistryLactate dehydrogenaseMaterials ChemistryDependenceEnzyme reaction mechanismchemistry.chemical_classificationL-Lactate DehydrogenaseMolecular StructureChemistryHydrideUNESCO::QUÍMICA::Química analíticaMetals and AlloysTitrimetryGeneral ChemistryNADL-Lactate dehydrogenaseSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsDependence ; Enzyme reaction mechanism ; Titratable residues ; L-Lactate dehydrogenase ; QM/MMEnzymeCeramics and Composites:QUÍMICA::Química analítica [UNESCO]Titratable residuesProtons

description

We have studied the dependence of the chemical reaction mechanism of L-lactate dehydrogenase (LDH) on the protonation state of titratable residues and on the level of the quantum mechanical (QM) description by means of hybrid quantum-mechanical/molecular-mechanical (QM/MM) methods; this methodology has allowed clarification of the timing of the hydride transfer and proton transfer components that hitherto had not been possible to state definitively. Ferrer Castillo, Silvia, Silvia.Ferrer@uv.es, Silla Santos, Estanislao, Estanislao.Silla@uv.es ; Tuñon Garcia de Vicuña, Ignacio Nilo, Ignacio.Tunon@uv.es

yearjournalcountryeditionlanguage
2005-12-01
http://hdl.handle.net/10550/16717