Multichannel circular dichroism investigations of the structural stability of bacterial cytochrome P-450.

The thermal unfolding of cytochrome P-450 LIN and P-450 CAM measured in presence and absence of their specific substrates was analyzed by circular dichroism (CD) and the alpha-helix content was estimated. Both proteins show, independent of the presence or absence of the substrates, nearly the same amount of loss of the CD in the peptide region. The comparison of the half transition temperatures determined from different chromophores and different methods indicates a non-two-state transition of the thermal unfolding. For such analysis we developed a new spectrometer, which is capable of measuring the CD simultaneously at all wavelengths in a limited wavelength region.