TY - JOUR
T1 - High-resolution multiwavelength surface plasmon resonance spectroscopy for probing conformational and electronic changes in redox proteins
AU - Boussaad, S.
AU - Pean, J.
AU - Tao, N. J.
PY - 2000/1/1
Y1 - 2000/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0033981950&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033981950&partnerID=8YFLogxK
U2 - 10.1021/ac990947n
DO - 10.1021/ac990947n
M3 - Article
C2 - 10655657
AN - SCOPUS:0033981950
SN - 0003-2700
VL - 72
SP - 222
EP - 226
JO - Analytical Chemistry
JF - Analytical Chemistry
IS - 1
ER -