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• W2062368218 abstract "The electron transfer-induced conformational changes in cytochrome c adsorbed on electrodes have been studied with high-resolution surface plasmon resonance spectroscopy. The conformational changes in the native protein follow a stretched exponential function, exp[−(t/τ)0.5], suggesting a distribution of the activation barrier heights in the process. The measured time constants, τ, are 0.21 and 0.14 s for the oxidation and reduction, respectively. They are much slower than the electron transfer process, due to structural relaxation of the protein layer. As the concentration of guanidine hydrochloride is increased to 3 M, the conformational changes diminish, which indicates that the electron-transfer center is decoupled from the rest of the protein. After replacing the denaturant with buffer, the conformational changes re-appear but occur with much slower time constants. The slowing-down of the conformational changes may be due to the trapping of the protein in an intermediate state." @default.
• W2062368218 created "2016-06-24" @default.
• W2062368218 creator A5012127347 @default.
• W2062368218 creator A5079960526 @default.
• W2062368218 date "2003-09-01" @default.
• W2062368218 modified "2023-10-03" @default.
• W2062368218 title "Kinetics of electron transfer-induced conformational changes in cytochrome c immobilized on electrodes studied with surface plasmon resonance" @default.
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• W2062368218 doi "https://doi.org/10.1016/s0022-0728(03)00197-9" @default.
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