The influence of the structure of the Au(110) surface on the ordering of a monolayer of cytochrome P450 reductase at the Au(110)/phosphate buffer interface-Reference-Cited by-同舟云学术

The influence of the structure of the Au(110) surface on the ordering of a monolayer of cytochrome P450 reductase at the Au(110)/phosphate buffer interface

Published:2013-10-30 Issue:3 Volume:251 Page:549-554
ISSN:0370-1972
Container-title:physica status solidi (b)
language:en
Short-container-title:Phys. Status Solidi B

Author:

Smith C. I.¹,Convery J. H.¹,Khara B.²,Scrutton N. S.²,Weightman P.¹

Affiliation:

1. Oliver Lodge Laboratory; Department of Physics; University of Liverpool; Liverpool L69 7ZE UK

2. Faculty of Life Sciences; Manchester Institute of Biotechnology; University of Manchester; 131 Princess Street Manchester M1 7DN UK

Publisher

Wiley

Subject

Condensed Matter Physics,Electronic, Optical and Magnetic Materials

Reference23 articles.

1. Controlling the formation of a monolayer of cytochrome P450 reductase onto Au surfaces

2. Evidence for protein conformational change at a Au(110)/protein interface

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

4. Electron transfer by diflavin reductases

5. Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes

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2. Ordered multilayers of cytochrome P450 reductase adsorbed at Au(110)/phosphate buffer interfaces;physica status solidi (b);2014-08-14

3. Conformational change in cytochrome P450 reductase adsorbed at a Au(110)—phosphate buffer interface induced by interaction with nicotinamide adenine dinucleotide phosphate;Physical Review E;2014-08-13