pH-dependent structural change of cytochrome-C

Effect of pH variation on the dynamic motion of cytochrome-C through conductivity, electronic absorption spectra and magnetic susceptibility coupled with molecular weight change were investigated. The very low pH region increases the probability of conversion native cytochrome-C to random coil. Neutralization leads to fold protein after being unfolded. Low spin state, mixture of low spin and high spin and high spin state of iron heme of cytochrome-C were demonstrated at acidic, neutral and alkali solution, respectively