title: New insights into enzyme catalysis. Ground state tunnelling driven by protein dynamics.
abstract: The wave-particle duality of matter suggests that quantum tunnelling may have a prominent role in enzymatic H-transfer. However, unlike for electron tunnelling, evidence for H-tunnelling in enzyme molecules is extremely limited. The theoretical development, and verification by experiment, of a role for protein dynamics in driving enzymatic H-tunnelling is presented. Dynamic theories of H-tunnelling suggest that the kinetic isotope effect, during rupture of a C-H/C-D bond, for example, can assume values interpreted previously as indicating classical transfer. Vibrationally enhanced ground state tunnelling has been demonstrated for enzymes that cleave stable C-H bonds. This is an attractive mechanism as large activation energies make it energetically unfavourable for a classical, over-the-barrier mode of cleavage. Furthermore, it may be a general strategy used by enzymes for catalysing these 'difficult' transformations.
authors.affiliation: Department of Biochemistry, University of Leicester, University Road, Leicester LE1 7RH, UK. nss4@le.ac.uk
authors.forename: N S
authors.initials: NS
authors.lastname: Scrutton
authors.forename: J
authors.initials: J
authors.lastname: Basran
authors.forename: M J
authors.initials: MJ
authors.lastname: Sutcliffe
mesh_terms: D000818:Animals; D002384:Catalysis; D004735:Energy Transfer; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D008956:Models, Chemical; D011789:Quantum Theory; D055672:Static Electricity; D013816:Thermodynamics
chemical_list: D004798:Enzymes