Interaction of ferricytochrome c with polyanion Nafion.
The properties of the complex of ferricyt c with fluorosulfonated polyanion Nafion (as a representative 'hydrophobic' polyanion) have been studied by means of optical spectroscopy and differential scanning calorimetry. The addition of the polyanion to a solution of ferricyt c (pH 7.4) resulted in an expansion of the protein molecule characterized by a profound decrease in enthalpy of the thermal transition of ferricyt c. The conformational change of ferricyt c upon addition of Nafion was shown by a perturbation of the Met-80-heme iron bond and an apparent increase in the distance of Trp-59 from the heme. The conformational change in the heme region was also observed by examining the CD spectra. The conformational state of ferricyt c in a complex with Nafion was similar to that designated as state II by Hildebrandt (Hildebrandt, P. (1990) Biochim. Biophys. Acta 1040, 175-186) in the complex with negatively charged heteropolytungstates-a six-coordinated low-spin state with a destabilized structure of the heme crevice. The decrease in enthalpy of the thermal transition of ferricyt c, the spectral changes in absorbance and the CD spectra, together with an increase in Trp fluorescence induced by Nafion addition observed at high ionic strength, all point to the involvement of the non-coulombic interaction.
Sedlák
E
E
Department of Biochemistry, Faculty of Science P. J. Safárik University, Kosice, Slovakia.
Antalík
M
M
Bágel'ová
J
J
Fedurco
M
M
D000818:Animals; D002152:Calorimetry, Differential Scanning; D003574:Cytochrome c Group / Q000737:chemistry* / Q000378:metabolism*; D005465:Fluorocarbon Polymers / Q000737:chemistry* / Q000378:metabolism* / Q000494:pharmacology; D006736:Horses; D007700:Kinetics; D009206:Myocardium; D011487:Protein Conformation / Q000187:drug effects; D013053:Spectrophotometry; D014364:Tryptophan
D003574:Cytochrome c Group; D005465:Fluorocarbon Polymers; C040402:perfluorosulfonic acid; D014364:Tryptophan