Protein dynamics: conformational disorder, vibrational coupling and anharmonicity in deoxy-hemoglobin and myoglobin.
In this work we study the temperature dependence of the Soret band lineshape of deoxymyoglobin and deoxyhemoglobin, in the range 300-20 K. To fit the measured spectra we use an approach originally proposed by Champion and coworkers (Srajer et al. 1986; Srajer and Champion 1991). The band profile is modelled as a Voigt function that accounts for the coupling with low frequency vibrational modes, whereas the coupling with high frequency modes is responsible for the vibronic structure of the spectra. Moreover, owing to the position of the iron atom out of the mean heme plane, inhomogeneous broadening brings about a non-Gaussian distribution of 0-0 electronic transition frequencies. The reported analysis enables us to isolate the various contributions to the overall bandwidth, and their temperature dependence points out the relevance of low frequency vibrations and of large scale anharmonic motions starting at temperatures higher than 170 K. Information on the mean iron-heme plane distance and on its temperature dependence, as well as on the heme pocket conformational disorder, is also obtained.
Cupane
A
A
Istituto di Fisica dell' Università, Palermo, Italy.
Leone
M
M
Vitrano
E
E
D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D006454:Hemoglobins / Q000737:chemistry*; D009211:Myoglobin / Q000737:chemistry*; D011487:Protein Conformation; D013053:Spectrophotometry; D013696:Temperature; D013816:Thermodynamics
D006454:Hemoglobins; D009211:Myoglobin; C018013:carboxymyoglobin; C100003:deoxyhemoglobin