INQUIMAE 12526
INSTITUTO DE QUIMICA, FISICA DE LOS MATERIALES, MEDIOAMBIENTE Y ENERGIA
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
High Pressure Reveals Structural Determinants for Globin Hexacoordination: Neuroglobin and Myoglobin cases
Autor/es:
LUCIANA CAPECE; MARCELO A. MARTI; ALEJANDRO D. NADRA; AXEL BIDON-CHANAL; F. JAVIER LUQUE; DARIO A. ESTRIN
Lugar:
St. Simons Island, Georgia, Atlanta, USA
Reunión:
Simposio; 49th Sanibel Symposium; 2009
Institución organizadora:
Quantum Theory Project - University of Florida
Resumen:
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The
influence of pressure on the equilibrium between five (5c) and
six-coordination (6c) forms in neuroglobin (Ngb) and myoglobin (Mb)
has been examined by means of molecular dynamics (MD) simulations at
normal and high pressure. The results show that the main effect of
high pressure is to reduce the protein mobility without altering the
structure in a significant manner. Moreover, our data suggest that
the equilibrium between 5c and 6c states in globins is largely
controlled by the structure and dynamics of the C-D region. Finally,
in agreement with the available experimental data, the free energy
profiles obtained from steered MD for both proteins indicate that
high pressure enhances hexacoordination. In Ngb the shift in
equilibrium is mainly relate to an increase in the 6c5c
transition barrier, whereas in Mb such a shift is primarily due to a
destabilization of the 5c state.
