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|Author(s):||T Petralli-Mallow; Anne L. Plant; M Lewis; J Hicks;|
|Title:||Cytochrome c at Model Membrane Surfaces: Exploration via Second Harmonic Generation - Circular Dichroism and Surface-Enhanced Resonance Raman Spectroscopy|
|Published:||July 11, 2000|
|Abstract:||The novel nonlinear optical method second harmonic generation-circular dichroism (SHG-CD) has been used to follow the adsorption and redox properties of a peripheral membrane protein horse heart cytochrome c, adsorbed at several model membrane surfaces. SHG-CD response is shown to be effected by the oxidation state of the heme within surface-adsorbed cytochrome c, as is consistent with the sensitivity of SHG to the chirality of the heme. SHG-CD measurements show that adsorbed cytochrome c is reducible by ascorbate at alkanethiol surfaces, but not at a phospholipid/alkanethiol hybrid bilayer membranes (HBMs). The adsorption of cytochrome c at the model membrane surfaces was verified by surface plasmon resonance. Surface enhanced resonance Raman measurements show that cytochrome c adsorbed on a hybrid bilayer membrane retains the Fe-heme conformation associated with solution-phase cytochrome c and is reducible by applying potential to the supporting electrode. The inability of ascorbic acid to reduce cytochrome c associated with the HBM is attributed not to a change in its redox potential, but rather to the nature of the interaction of cytochrome c with the HBM.|
|Pages:||pp. 5960 - 5966|
|Keywords:||cytochrome c,hybrid bilayer membrane,nonlinear optics,second harmonic generation,surface enhanced resonance Raman|
|Research Areas:||Spectroscopy, Life Sciences Research, Raman|