Ordered multilayers of cytochrome P450 reductase adsorbed at Au(110)/phosphate buffer interfaces

C. I. Smith; J. H. Convery; B. Khara; N. S. Scrutton; P. Weightman

doi:10.1002/pssb.201451221

Ordered multilayers of cytochrome P450 reductase adsorbed at Au(110)/phosphate buffer interfaces

C. I. Smith, J. H. Convery, B. Khara, N. S. Scrutton, P. Weightman

Research output: Contribution to journal › Article › peer-review

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. © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Original language	English
Journal	Physica Status Solidi (B) Basic Research
DOIs	https://doi.org/10.1002/pssb.201451221
Publication status	Published - 2014

Keywords

Cytochrome P450 reductase
Gold
Protein dynamics
Reflection anisotropy spectroscopy

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10.1002/pssb.201451221

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title = "Ordered multilayers of cytochrome P450 reductase adsorbed at Au(110)/phosphate buffer interfaces",

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. {\textcopyright} 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",

keywords = "Cytochrome P450 reductase, Gold, Protein dynamics, Reflection anisotropy spectroscopy",

author = "Smith, {C. I.} and Convery, {J. H.} and B. Khara and Scrutton, {N. S.} and P. Weightman",

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doi = "10.1002/pssb.201451221",

language = "English",

journal = "Physica Status Solidi (B) Basic Research",

issn = "0370-1972",

publisher = "John Wiley & Sons Ltd",

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T1 - Ordered multilayers of cytochrome P450 reductase adsorbed at Au(110)/phosphate buffer interfaces

AU - Smith, C. I.

AU - Convery, J. H.

AU - Khara, B.

AU - Scrutton, N. S.

AU - Weightman, P.

PY - 2014

Y1 - 2014

N2 - 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. © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

AB - 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. © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

KW - Cytochrome P450 reductase

KW - Gold

KW - Protein dynamics

KW - Reflection anisotropy spectroscopy

U2 - 10.1002/pssb.201451221

DO - 10.1002/pssb.201451221

M3 - Article

SN - 0370-1972

JO - Physica Status Solidi (B) Basic Research

JF - Physica Status Solidi (B) Basic Research

ER -

Ordered multilayers of cytochrome P450 reductase adsorbed at Au(110)/phosphate buffer interfaces

Abstract

Keywords

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