Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/106243
Title: Two-dimensional heterospectral correlation analysis of the redox-induced conformational transition in cytochrome c using surface-enhanced Raman and infrared absorption spectroscopies on a two-layer gold surface
Authors: Zou, Changji
Larisika, Melanie
Nagy, Gabor
Srajer, Johannes
Oostenbrink, Chris
Chen, Xiaodong
Knoll, Wolfgang
Nowak, Christoph
Bo, Liedberg
Keywords: surface-enhanced Raman spectroscopy
redox protein
Two-layer gold surface
2D heterospectral correlation spectroscopy
cytochrome c
surface-enhanced infrared absorption spectroscopy
DRNTU::Engineering::Materials
Issue Date: 2013
Source: Zou, C., Larisika, M., Nagy, G., Srajer, J., Oostenbrink, C., Chen, X., et al. (2013). Two-dimensional heterospectral correlation analysis of the redox-induced conformational transition in cytochrome c using surface-enhanced raman and infrared absorption spectroscopies on a two-layer gold surface. The journal of physical chemistry B, 117(33), 9606-9614.
Series/Report no.: The journal of physical chemistry B
Abstract: The heme protein cytochrome c adsorbed to a two-layer gold surface modified with a self-assembled monolayer of 2-mercaptoethanol was analyzed using a two-dimensional (2D) heterospectral correlation analysis that combined surface-enhanced infrared absorption spectroscopy (SEIRAS) and surface-enhanced Raman spectroscopy (SERS). Stepwise increasing electric potentials were applied to alter the redox state of the protein and to induce conformational changes within the protein backbone. We demonstrate herein that 2D heterospectral correlation analysis is a particularly suitable and useful technique for the study of heme-containing proteins as the two spectroscopies address different portions of the protein. Thus, by correlating SERS and SEIRAS data in a 2D plot, we can obtain a deeper understanding of the conformational changes occurring at the redox center and in the supporting protein backbone during the electron transfer process. The correlation analyses are complemented by molecular dynamics calculations to explore the intramolecular interactions.
URI: https://hdl.handle.net/10356/106243
http://hdl.handle.net/10220/17762
DOI: 10.1021/jp404573q
Rights: © 2013 American Chemical Society (ACS). This is the author created version of a work that has been peer reviewed and accepted for publication by The Journal of Physical Chemistry B, American Chemical Society (ACS). It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1021/jp404573q].
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:MSE Journal Articles

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