title: Conformational change induced by electron transfer in a monolayer of cytochrome P450 reductase adsorbed at the Au(110)-phosphate buffer interface.
abstract: The reflection anisotropy spectroscopy profiles of a variant of cytochrome P450 reductase adsorbed at the Au(110)-phosphate buffer interface depend on the sequence of potentials applied to the Au(110) electrode. It is suggested that this dependence arises from changes in the orientation of the isoalloxazine ring structures in the protein with respect to the Au(110) surface. This offers a method of monitoring conformational change in this protein by measuring variations in the reflection anisotropy spectrum arising from changes in the redox potential.
authors.affiliation: Department of Physics, Oliver Lodge Laboratory, University of Liverpool, Liverpool L69 7ZE, United Kingdom.
authors.forename: P
authors.initials: P
authors.lastname: Weightman
authors.forename: C I
authors.initials: CI
authors.lastname: Smith
authors.forename: J H
authors.initials: JH
authors.lastname: Convery
authors.forename: P
authors.initials: P
authors.lastname: Harrison
authors.forename: B
authors.initials: B
authors.lastname: Khara
authors.forename: N S
authors.initials: NS
authors.lastname: Scrutton
mesh_terms: D000327:Adsorption; D016880:Anisotropy; D002021:Buffers; D004566:Electrodes; D004579:Electron Transport; D006046:Gold / Q000737:chemistry*; D008958:Models, Molecular; D009251:NADPH-Ferrihemoprotein Reductase / Q000737:chemistry*; D010710:Phosphates / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D002021:Buffers; D010710:Phosphates; D006046:Gold; D009251:NADPH-Ferrihemoprotein Reductase