Evidence for protein conformational change at a Au(110)/protein interfaceH. L. Messiha1, C. I. Smith2, N. S. Scrutton1 and P. Weightman2
1 Faculty of Life Sciences, University of Manchester, Manchester Interdisciplinary Biocentre 131 Princess Street, Manchester, M1 7ND, UK, EU
2 Department of Physics, University of Liverpool - Liverpool, L69 7ZE, UK, EU
received 14 January 2008; accepted in final form 22 May 2008; published July 2008
published online 19 June 2008
Evidence is presented that reflection anisotropy spectroscopy (RAS) can provide real-time measurements of conformational change in proteins induced by electron transfer reactions. A bacterial electron transferring flavoprotein (ETF) has been modified so as to adsorb on an Au(110) electrode and enable reversible electron transfer to the protein cofactor in the absence of mediators. Reversible changes are observed in the RAS of this protein that are interpreted as arising from conformational changes accompanying the transfer of electrons.
87.80.Dj - Spectroscopies.
81.16.Dn - Self-assembly.
82.45.Tv - Bioelectrochemistry.
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