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Ordered multilayers of cytochrome P450 reductase adsorbed at Au(110)/phosphate buffer interfaces
Author(s) -
Smith C. I.,
Convery J. H.,
Khara B.,
Scrutton N. S.,
Weightman P.
Publication year - 2015
Publication title -
physica status solidi (b)
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.51
H-Index - 109
eISSN - 1521-3951
pISSN - 0370-1972
DOI - 10.1002/pssb.201451221
Subject(s) - bilayer , adsorption , dipole , phosphate , reflection (computer programming) , substrate (aquarium) , crystallography , phosphate buffered saline , chemistry , anisotropy , materials science , analytical chemistry (journal) , membrane , optics , physics , biochemistry , oceanography , organic chemistry , chromatography , computer science , programming language , geology
Bilayers and multilayers of a mutated form of cytochrome P450 reductase, P499C, form ordered structures when adsorbed at Au(110)/phosphate buffer interfaces. Reflection anisotropy spectroscopy (RAS) indicates that the degree of order increases with the number of layers and that the optical dipoles that contribute to the RAS profiles observed from the bilayer lie in planes that are oriented vertical to the surface and along one of the principal axes of the Au(110) surface. The contribution of the Au(110) substrate and the protein to the RAS profiles of the combined systems show an opposite dependence on the potential applied to the Au(110) electrode. The RAS profile observed from an adsorbed multilayer is dominated by the contribution from the protein.