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Redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced infrared absorption spectroscopy
Citation key ISI:000258738200015
Author Wisitruangsakul, Nattawadee and Zebger, Ingo and Ly, Khoa H. and Murgida, Daniel H. and Ekgasit, Sanong and Hildebrandt, Peter
Pages 5276-5286
Year 2008
ISSN 1463-9076
DOI 10.1039/b806528d
Address THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND
Journal Phys. chem. chem. phys
Volume 10
Number 34
Publisher ROYAL SOC CHEMISTRY
Abstract Time-resolved surface enhanced infrared absorption (SEIRA) spectroscopy is employed to analyse the dynamics of the protein structural changes coupled to the electron transfer process of immobilised cytochrome c (Cyt-c). Upon electrostatic binding of Cyt-c to Au electrodes coated with self-assembled monolayers (SAMs) of carboxyl-terminated thiols, cyclic voltammetric measurements demonstrate a reversible redox process with a redox potential that is similar to that of Cyt-c in solution, and a non-exponential distance-dependence of the electron transfer rate as observed previously (D. H. Murgida and P. Hildebrandt, Chem. Soc. Rev. 2008, 37, 937). On the basis of characteristic redox-state-sensitive amide I bands, the protein structural changes triggered by the electron transfer are monitored by rapid scan and step scan SEIRA spectroscopy in combination with the potential jump technique. Whereas the temporal evolution of the conjugate bands at 1693 and 1673 cm(-1) displays the same rate constants as electron transfer, the time-dependent changes of the 1660-cm(-1) band are slower by about a factor of 2. The study demonstrates that time-resolved SEIRA spectroscopy provides further information about the dynamics and mechanism of interfacial processes of redox proteins, thereby complementing the results obtained from other surface-sensitive techniques. In comparison with previous surface enhanced resonance Raman spectroscopic findings, the present results are discussed in terms of the local electric field strengths at the Au/SAM/Cyt-c interface.
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