Preliminary spectrofluoroelectrochemical studies indicate a possible conformational change in horse heart cytochrome c upon reduction
| Autor: | William R. Heineman, George P. Kreishman, Michael J. Simone |
|---|---|
| Rok vydání: | 1982 |
| Předmět: |
Conformational change
Quenching (fluorescence) biology Chemistry Cytochrome c Tryptophan Spectrofluorometer Photochemistry Fluorescence Surfaces Coatings and Films Electronic Optical and Magnetic Materials Biomaterials chemistry.chemical_compound Colloid and Surface Chemistry Electrode biology.protein Heme |
| Zdroj: | Journal of Colloid and Interface Science. 86:295-298 |
| ISSN: | 0021-9797 |
| Popis: | An optically transparent thin-layer electrode can be used in conjunction with a spectrofluorometer to monitor the changes in the fluorescence properties of tryptophan-59 of horse heart cytochrome c as a function of applied solution potential. The fluorescence spectrum for the reduced state differs from that of the oxidized state. Several factors attenuated the fluorescence of the tryptophan, namely, (1) energy transfer of the fluorescence to the heme and (2) because of the high concentrations used in these studies, the fluorescence is decreased by quenching by other cytochrome c's in solution. Taking these two factors into account, the observed fluorescence intensities at a given wavelength can be explained if one assumes a movement of the tryptophan toward the heme of 0.7 ± 0.3 A upon reduction. |
| Databáze: | OpenAIRE |
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