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FTIR study demonstrates structural changes in ferricytochrome c across varying pH levels, indicating important biochemical implications.
The spectra of amide I region (1700-1600cm-1) of horse heart ferricytochrome c at 20oC are reported at low ionic strength at of pH values between 7.0 and 11.5 encompassing the alkaline transition. The mid-infrared spectra can probe the protein secondary structures. The Fourier transform infrared spectroscopic technique is used to investigate the changes in the conformationally sensitive amide I band of cytochrome c with pH and ionic strength. Analysis of these results supports the hypothesis that an increase in the non-repetitive secondary structure during alkaline transition is at the expense of regular secondary structures. These strongly suggest that structural switching and ligand exchange behaviour of ferricytochrome c is accompanied by conformational change in the protein backbone
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Wasagu et al. (2011) studied this question.
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