Transient resonance Raman evidence for structural reorganizational dynamics during electron transfer in ruthenated yeast cytochrome c

The characteristics of structural dynamics of the heme and its surrounding proteins in yeast cytochrome c is investigated by using time-resolved resonance Raman spectroscopy and transient resonance Raman spectroscopy. The yeast cytochrome c is ruthenated at Cys-102 (RuC). The investigation reveals that the protein functions as a nonspecific dielectric solvent. The resonance Raman spectroscopy reveals the influence of the heme on its surrounding proteins during their functioning.