Abstract
Surface-Enhanced Raman Scattering (SERS) spectra of [Ru(CN)5(pyS)]4− (RupyS) complex self-assembled monolayer (SAM) were obtained on gold and silver surfaces at 632.8 and 413.1 nm excitation radiations, respectively. The bands assigned to the heme iron of the cytochrome c (cyt c) metalloprotein group were observed by using the RupyS SAM on silver at 413.1 nm. The Surface-Enhanced Resonance Raman Scattering (SERRS) spectra of the RupyS SAM on silver in the cyt c solution obtained at −0.2 and +0.2 V present bands at 1,365 and 1,374 cm−1 characteristic of the heme group, indicating the reduced and oxidized states of this protein, respectively. The bands observed at 1,464, 1,504, and 1,638 cm−1 are used to confirm the redox state of cyt c. The presence of the oxidized and reduced bands in function of different applied potential is an evidence that the protein is interacting with the modifier.
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The authors I. C. N. Diógenes, I. S. Moreira, and M. L. A. Temperini would like to express their thankfulness to “Conselho Nacional de Desenvolvimento Científico e Tecnológico” (CNPq) for grants.
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This paper is dedicated to Prof. Francisco Nart, in memoriam.
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Diógenes, I.C.N., Nart, F.C., Barreto, M.B.P.M. et al. SERRS study of [Ru(CN)5(pyS)]4− SAM and cytochrome c: A suggestion toward the heterogeneous molecular recognition. J Solid State Electrochem 11, 1585–1590 (2007). https://doi.org/10.1007/s10008-007-0366-5
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DOI: https://doi.org/10.1007/s10008-007-0366-5