Local dynamic properties of the heme pocket in native and solvent-induced molten-globule-like states of cytochrome c.
We report the Soret absorption band, down to cryogenic temperature, of native and molten-globule-like state of horse heart cytochrome c. The band profile is analyzed in terms of vibronic coupling of the heme normal modes to the electronic transition in the framework of the Franck-Condon approximation. From the temperature dependence of the Gaussian broadening and of the peak position, we obtain information on the 'bath' of low frequency harmonic motions of the heme group within the heme pocket. The reported data indicate that, compared to the native state, the less rigid tertiary structure of the molten globule is reflected in a higher flexibility of the heme pocket and in greater conformational disorder, allowing the transduction of large-amplitude motion of the protein to the dynamics of the heme pocket.
Militello
V
V
Istituto Nazionale per la Fisica della Materia and Dipartimento di Medicina Sperimentale, University of Palermo, Corso Tukory 129, Palermo, Italy. militello@fisica.unipa.it
Leone
M
M
Cupane
A
A
Santucci
R
R
Desideri
A
A
D001665:Binding Sites; D003574:Cytochrome c Group / Q000737:chemistry*; D005990:Glycerol / Q000737:chemistry; D006418:Heme / Q000737:chemistry*; D006358:Hot Temperature; D008433:Mathematics; D011487:Protein Conformation; D017510:Protein Folding; D013057:Spectrum Analysis
D003574:Cytochrome c Group; D006418:Heme; D005990:Glycerol