1. Ordered multilayers of cytochrome P450 reductase adsorbed at Au(110)/phosphate buffer interfaces.
- Author
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Smith, C. I., Convery, J. H., Khara, B., Scrutton, N. S., and Weightman, P.
- Subjects
CYTOCHROME P-450 ,GOLD ,FLAVIN adenine dinucleotide ,FLAVIN mononucleotide ,ATOMIC force microscopy ,QUARTZ crystal microbalances ,PHOSPHATES - Abstract
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. [ABSTRACT FROM AUTHOR]
- Published
- 2015
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