About this Journal Submit a Manuscript Table of Contents
Spectroscopy
Volume 24 (2010), Issue 1-2, Pages 125-129
http://dx.doi.org/10.3233/SPE-2010-0414

Time-resolved surface-enhanced resonance Raman spectro-electrochemistry of heme proteins

Marc Grosserueschkamp,1,2 Christoph Nowak,1,2 Wolfgang Knoll,2 and Renate L. C. Naumann1,2,3

1Max Planck Institute for Polymer Research, Mainz, Germany
2Austrian Research Centers GmbH, Tech Gate Vienna, Vienna, Austria
3Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany

Copyright © 2010 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Heme proteins such as cytochrome c (cc) play a fundamental role in many biological processes. Surface-enhanced resonance Raman spectroscopy (SERRS) combined with electrochemical methods is an ideal tool to study the redox processes of heme proteins. In this context we designed a new measuring cell allowing for simultaneous electrochemical manipulation and high sensitive SERRS measurements of heme proteins. The measuring cell is based on an inverted rotating disc electrode for excitation by using a confocal Raman microscope. Furthermore, we developed a SER(R)S-active silver modified silver substrate for spectro-electrochemical applications. For this purpose silver nanoparticles (AgNPs) were adsorbed on top of a planar silver surface. The substrate was optimized for an excitation wavelength of 413 nm corresponding to the resonance frequency of heme structures. An enhancement factor of 105 was achieved. The high performance of the new measuring cell in combination with the new silver substrate was demonstrated using cc as a reference system.