title: Free-energy landscape of enzyme catalysis.
abstract: The concept is developed that enzyme mechanisms should be viewed as "catalytic networks" with multiple conformations that occur serially and in parallel in the mechanism. These coupled ensembles of conformations require a multi-dimensional standard free-energy surface that is very "rugged", containing multiple minima and transition states. Experimental and theoretical evidence is presented to support this concept.
authors.affiliation: Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.
authors.forename: Stephen J
authors.initials: SJ
authors.lastname: Benkovic
authors.forename: Gordon G
authors.initials: GG
authors.lastname: Hammes
authors.forename: Sharon
authors.initials: S
authors.lastname: Hammes-Schiffer
mesh_terms: D002384:Catalysis; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D011487:Protein Conformation; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D013816:Thermodynamics
chemical_list: D029968:Escherichia coli Proteins; D013762:Tetrahydrofolate Dehydrogenase