Structure-dynamics-function relationships in Asian elephant (Elephas maximus) myoglobin. An optical spectroscopy and flash photolysis study on functionally important motions
| Autor: | W. Yu, Lorenzo Cordone, Maurizio Leone, E. E. Di Iorio, Eugenio Vitrano, Antonio Cupane, U.R. Hiltpold, K.H. Winterhalter |
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| Rok vydání: | 1993 |
| Předmět: |
Voigt profile
Photolysis Myoglobin Protein Conformation Photodissociation Elephants Analytical chemistry Electron Spin Resonance Spectroscopy Biophysics Soft modes Molecular electronic transition chemistry.chemical_compound Structure-Activity Relationship chemistry Carboxyhemoglobin Chemical physics Spectrophotometry Molecular vibration Flash photolysis Animals Thermodynamics Horses Spectroscopy Research Article |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 0006-3495 |
| DOI: | 10.1016/s0006-3495(93)81311-0 |
| Popis: | In this work we report the thermal behavior (10–300 K) of the Soret band lineshape of deoxy and carbonmonoxy derivatives of Asian elephant (Elephas maximus) and horse myoglobins together with their carbon monoxide recombination kinetics after flash photolysis; the results are compared to analogous data relative to sperm whale myoglobin. The Soret band profile is modeled as a Voigt function that accounts for the coupling with high and low frequency vibrational modes, while inhomogeneous broadening is taken into account with suitable distributions of purely electronic transition frequencies. This analysis makes it possible to isolate the various contributions to the overall lineshape that; in turn, give information on structural and dynamic properties of the systems studied. The optical spectroscopy data point out sizable differences between elephant myoglobin on one hand and horse and sperm whale myoglobins on the other. These differences, more pronounced in deoxy derivatives, involve both the structure and dynamics of the heme pocket; in particular, elephant myoglobin appears to be characterized by larger anharmonic contributions to soft modes than the other two proteins. Flash photolysis data are analyzed as sums of kinetic processes with temperature-dependent fractional amplitudes, characterized by discrete pre-exponentials and either discrete or distributed activation enthalpies. In the whole temperature range investigated the behavior of elephant myoglobin appears to be more complex than that of horse and sperm whale myoglobins, which is in agreement with the increased anharmonic contributions to soft modes found in the former protein. Thus, to satisfactorily fit the time courses for CO recombination to elephant myoglobin five distinct processes are needed, only one of which is populated over the whole temperature range investigated. The remarkable convergence and complementarity between optical spectroscopy and flash photolysis data confirms the utility of combining these two experimental techniques in order to gain new and deeper insights into the functional relevance of protein fluctuations. |
| Databáze: | OpenAIRE |
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