Evidence for protein conformational change at a Au(110)/protein interface.
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.
Messiha
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HL
Faculty of Life Sciences, University of Manchester, Manchester Interdisciplinary Biocentre 131 Princess Street, Manchester, M1 7ND, UK, EU.
Smith
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CI
Scrutton
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Weightman
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