High-resolution multiwavelength surface plasmon resonance spectroscopy for probing conformational and electronic changes in redox proteins

S. Boussaad, J. Pean, N. J. Tao

Research output: Contribution to journalArticlepeer-review

142 Scopus citations

Abstract

To date, surface plasmon resonance (SPR) spectroscopy identifies molecules via specific bindings with their ligands immobilized on a surface. We demonstrate here that a high-resolution multiwavelength SPR technique can measure the electronic states of the molecules and thus allow direct identification of the molecules. Using this new capability, we have studied the electronic and conformational differences between the oxidized and reduced states of cytochrome c immobilized on a modified gold electrode. When the wavelength of the incident light is far away from the optical absorption bands of the protein, a ~0.008°decrease in the resonance angle, due to a conformational change, occurs as the protein is switched from the oxidized to reduced states. When the wavelength is tuned to the absorption bands, the resonance angle oscillates at the wavelengths of the absorption peaks, which provides electronic signatures of the protein.

Original languageEnglish (US)
Pages (from-to)222-226
Number of pages5
JournalAnalytical chemistry
Volume72
Issue number1
DOIs
StatePublished - Jan 1 2000
Externally publishedYes

ASJC Scopus subject areas

  • Analytical Chemistry

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