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• W2016126230 abstract "The structural stability and redox properties of yeast iso-1-cytochrome c and its mutant, F82H, were studied by surface-enhanced resonance Raman scattering (SERRS) spectroscopy. Phenylalanine, which exists at the position-82 in yeast iso-1-cytochrome c, is replaced by histidine in the mutant. The SERRS spectra of the proteins on the bare silver electrodes indicate that the mutant possesses a more stable global structure with regard to the adsorption-induced conformational alteration. The redox potential of the mutant negatively shifts by about 400 mV, relative to that of yeast iso-1-cytochrome c. This is ascribed to axial ligand switching and higher solvent accessibility of the heme iron in the mutant during the redox reactions." @default.
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• W2016126230 date "2002-07-01" @default.
• W2016126230 modified "2023-10-18" @default.
• W2016126230 title "Surface-enhanced resonance Raman spectroscopic study of yeast iso-1-cytochrome c and its mutant" @default.
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• W2016126230 doi "https://doi.org/10.1016/s0022-0728(02)01003-3" @default.
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