title: Conformational reorganisation in interfacial protein electron transfer.
abstract: Protein-protein electron transfer (ET) plays an essential role in all redox chains. Earlier studies which used cross-linking and increased solution viscosity indicated that the rate of many ET reactions is limited (i.e., gated) by conformational reorientations at the surface interface. These results are later supported by structural studies using NMR and molecular modelling. New insights into conformational gating have also come from electrochemical experiments in which proteins are noncovalently adsorbed on the electrode surface. These systems have the advantage that it is relatively easy to vary systematically the driving force and electronic coupling. In this review we summarize the current knowledge obtained from these electrochemical experiments and compare it with some of the results obtained for protein-protein ET.
authors.affiliation: Physics and Astronomy, University of Leeds, UK. L.J.C.Jeuken@leeds.ac.uk
authors.forename: Lars J C
authors.initials: LJ
authors.lastname: Jeuken
mesh_terms: D004563:Electrochemistry; D004566:Electrodes; D004579:Electron Transport; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism; D015640:Ion Channel Gating; D007700:Kinetics; D008954:Models, Biological; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013816:Thermodynamics
chemical_list: D004798:Enzymes; D011506:Proteins