Conformational change induced by electron transfer in a monolayer of cytochrome P450 reductase adsorbed at the Au(110)-phosphate buffer interface

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

doi:10.1103/PhysRevE.88.032715

Conformational change induced by electron transfer in a monolayer of cytochrome P450 reductase adsorbed at the Au(110)-phosphate buffer interface

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

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

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. © 2013 American Physical Society.

Original language	English
Article number	032715
Journal	Physical Review E - Statistical, Nonlinear, and Soft Matter Physics
Volume	88
Issue number	3
DOIs	https://doi.org/10.1103/PhysRevE.88.032715
Publication status	Published - 26 Sept 2013

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Weightman, P., Smith, C. I., Convery, J. H., Harrison, P., Khara, B., & Scrutton, N. S. (2013). Conformational change induced by electron transfer in a monolayer of cytochrome P450 reductase adsorbed at the Au(110)-phosphate buffer interface. Physical Review E - Statistical, Nonlinear, and Soft Matter Physics, 88(3), Article 032715. https://doi.org/10.1103/PhysRevE.88.032715

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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. {\textcopyright} 2013 American Physical Society.",

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Conformational change induced by electron transfer in a monolayer of cytochrome P450 reductase adsorbed at the Au(110)-phosphate buffer interface. / Weightman, P.; Smith, C. I.; Convery, J. H. et al.
In: Physical Review E - Statistical, Nonlinear, and Soft Matter Physics, Vol. 88, No. 3, 032715, 26.09.2013.

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

TY - JOUR

T1 - Conformational change induced by electron transfer in a monolayer of cytochrome P450 reductase adsorbed at the Au(110)-phosphate buffer interface

AU - Weightman, P.

AU - Smith, C. I.

AU - Convery, J. H.

AU - Harrison, P.

AU - Khara, B.

AU - Scrutton, N. S.

PY - 2013/9/26

Y1 - 2013/9/26

N2 - 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. © 2013 American Physical Society.

AB - 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. © 2013 American Physical Society.

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DO - 10.1103/PhysRevE.88.032715

M3 - Article

SN - 1539-3755

VL - 88

JO - Physical Review E - Statistical, Nonlinear, and Soft Matter Physics

JF - Physical Review E - Statistical, Nonlinear, and Soft Matter Physics

IS - 3

M1 - 032715

ER -

Conformational change induced by electron transfer in a monolayer of cytochrome P450 reductase adsorbed at the Au(110)-phosphate buffer interface

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