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    STUDIA PHYSICA - Issue no. SPECIAL ISSUE / 2001  
         
  Article:   EPR INVESTIGATIONS OF NON COVALENT SPIN LABELLED CYTOCHROME C AND OVALBUMIN.

Authors:  G. DAMIAN, S. CAVALU, M. DÂNÅžOREANU, S. SIMON, C.M. LUCACIU. 		 
       
         
  Abstract:  Nitroxide radicals exhibit a number of chemical and physical properties that make them extremely useful molecules for studying biochemical systems, especially the metalloporphyrins. The aim of this work was to investigate the Tempyo spin label as a report group for the interactions and the conformational changes of lyophilized Cytochrome c and Ovalbumin, as function of pH. values in the range 2.5÷12. The EPR spectra are similar with those of other noncovalently spin label porphyrins in frozen solution at very low temperatures. This behavior indicated a possible spin-spin interaction between the hemic iron and the nitroxide group. The changes in the EPR spectra as function of the pH are discussed in terms of conformational changes of the proteins.  
         
     
         
         
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