Structural evaluation of cytochrome c by Raman spectroscopy and its relationship with apoptosis and protein degradation in postmortem bovine muscle

Structural changes of cytochrome c and its relationship with apoptosis and protein degradation of bovine muscle during postmortem aging were investigated. Results from amide I and amide II - VI showed that the pi* orbital d electron decreased, the pi electron density increased, and the frequency of the C-N stretching vibration increased. The distance between heme Fe and N atoms of the porphyrin decreased, the bond length decreased, and the heme core size decreased. Besides, Fe ligand vibration related Raman bands of cytochrome c had red (right) shift gradually with the extension of aging. The apoptotic rate and the degradation products of desmin and troponin-T were increased (P < 0.05). Correlation analysis results suggested that Fe ligand vibration, not amide I - VI related Raman bands were correlated with cytochrome c mediated apoptosis and degradation of myofibrillar protein of bovine muscle during aging.

Automated summary

The structural changes of cytochrome c in bovine muscle during postmortem aging were investigated, with results showing correlations between Fe ligand vibrations and apoptosis and protein degradation. The study found that as aging progressed, the pi* orbital d electron decreased, the pi electron density increased, and the frequency of the C-N stretching vibration increased. Additionally, the distance between heme Fe and N atoms of the porphyrin decreased, the bond length decreased, and the heme core size decreased.