INSTITUTO DE QUIMICA, FISICA DE LOS MATERIALES, MEDIOAMBIENTE Y ENERGIA
Unidad Ejecutora - UE
congresos y reuniones científicas
Dioxygen affinity in Heme Proteins Investigated by Computer Simulation
MARCELO A. MARTI; LUCIANA CAPECE; LEONARDO BOECHI; DAMIAN E. BIKIEL; DARIO A. ESTRIN
Congreso; 6th International Conference of Biological Physics - 5th Southern Cone Biophysical Congress - 34th Annual meeting of the Argentinian Biophysical Society.; 2007
We present an investigation of the molecular basis of the modulation of oxygen affinity in heme proteins using computer simulation. QM-MM calculations are applied to explore distal and proximal effects on O2 binding to the heme, while classical molecular dynamics simulations are employed to investigate ligand migration across the polypeptide to the active site. Trends in binding energies and in the kinetic constants are illustrated through a number of selected examples highlighting the virtues and the limitations of the applied methodologies. These examples cover a wide range of O2-affinities, and include: the truncated-N and truncated-O hemoglobins from Mycobacterium Tuberculosis, the mammalian muscular O2 storage protein: myoglobin, the hemoglobin from the parasitic nematode Ascaris lumbricoides, the oxygen transporter in the root of leguminous plants: Leghemoglobin, the Cerebratulus lacteus nerve tissue hemoglobin, and the Alcaligenes xyloxidans cytochrome c.