time-resolved surface-enhanced resonance raman spectro-electrochemistry of heme proteins时间分辨的表面增强共振喇曼spectro-electrochemistry血红素蛋白质.pdfVIP

Spectroscopy 24 (2010) 125–129 125 DOI 10.3233/SPE-2010-0414 IOS Press Time-resolved surface-enhanced resonance Raman spectro-electrochemistry of heme proteins Marc Grosserueschkamp a,b , Christoph Nowak a,b , Wolfgang Knoll b and Renate L.C. Naumann a,∗ a Max Planck Institute for Polymer Research, Mainz, Germany b Austrian Research Centers GmbH, Tech Gate Vienna, Vienna, Austria 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 5 structures. An enhancement factor of 10 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. Keywords: Time-resolved surface-enhanced resonance Raman spectroscopy, localized surface plasmons, silver, nanoparticles, electron transfer 1. Introduction Electron transfer kinetics of heme proteins adsorbed on metal surfaces can be investigated by spectro- electrochemistry [3,7]. A combination of surface-enhanced Raman scattering (SERS) and resonance Raman scattering (RRS)