title: Conformational change in cytochrome P450 reductase adsorbed at a Au(110)-phosphate buffer interface induced by interaction with nicotinamide adenine dinucleotide phosphate.
abstract: Changes observed in the reflection anisotropy spectroscopy (RAS) profiles of monolayers of cytochrome P450 reductase adsorbed at Au(110)-electrolyte interfaces at 0.056 V following the addition of nicotinamide adenine dinucleotide phosphate (NADP(+)) are explained in terms of a simple model as arising from changes in the orientation of an isoalloxazine ring located in the flavin mononucleotide binding domain of the protein. The model also accounts for the changes observed in the RAS as the potential applied to the Au(110) surface is varied and suggests that differences in the dependence of the RAS profile of the adsorbed protein on the potential applied to the electrode in the absence and presence of NADP(+) are explicable as arising from a competition between the applied potential acting to reduce the protein and the NADP(+) to oxidize it.
authors.affiliation: Department of Physics, Oliver Lodge Laboratory, University of Liverpool, Liverpool, L69 7ZE, United Kingdom.
authors.forename: C I
authors.initials: CI
authors.lastname: Smith
authors.affiliation: Department of Physics, Oliver Lodge Laboratory, University of Liverpool, Liverpool, L69 7ZE, United Kingdom.
authors.forename: J H
authors.initials: JH
authors.lastname: Convery
authors.affiliation: Department of Physics, Oliver Lodge Laboratory, University of Liverpool, Liverpool, L69 7ZE, United Kingdom.
authors.forename: P
authors.initials: P
authors.lastname: Harrison
authors.affiliation: Faculty of Life Sciences, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester, M1 7DN, United Kingdom.
authors.forename: B
authors.initials: B
authors.lastname: Khara
authors.affiliation: Faculty of Life Sciences, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester, M1 7DN, United Kingdom.
authors.forename: N S
authors.initials: NS
authors.lastname: Scrutton
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
mesh_terms: D004138:Dinitrocresols / Q000737:chemistry; D004573:Electrolytes / Q000737:chemistry*; D006046:Gold / Q000737:chemistry*; D008958:Models, Molecular; D009249:NADP / Q000737:chemistry*; D009251:NADPH-Ferrihemoprotein Reductase / Q000737:chemistry*; D010084:Oxidation-Reduction; D010710:Phosphates / Q000737:chemistry; D011487:Protein Conformation; D013057:Spectrum Analysis; D013499:Surface Properties
chemical_list: D004138:Dinitrocresols; D004573:Electrolytes; D010710:Phosphates; C024132:4,6-dinitro-o-cresol; D009249:NADP; D006046:Gold; D009251:NADPH-Ferrihemoprotein Reductase