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Secondary Structures Associated With Alkaline Transition of Horse Heart Ferricytochrome C: An FTIR Study


RSU Wasagu
MK Abubakar
M Lawal
CH Njoku

Abstract

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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eISSN: 2756-4843