INQUIMAE   12526
INSTITUTO DE QUIMICA, FISICA DE LOS MATERIALES, MEDIOAMBIENTE Y ENERGIA
Unidad Ejecutora - UE
artículos
Título:
The role of residue Thr122 of methylamine dehydrogenase on the proton transfer from the iminoquinone intermediate to residue Asp76
Autor/es:
GUSTAVO PIERDOMINICI-SOTTILE; MARCELO A. MARTI; JULIANA PALMA
Revista:
CHEMICAL PHYSICS LETTERS
Editorial:
Elsevier
Referencias:
Año: 2008 p. 243 - 243
ISSN:
0009-2614
Resumen:
We present the results of combined molecular dynamics and full-quantum calculations aimed at eluci-dating the role of residue Thr122 of the enzyme methylamine dehydrogenase. Calculations were per-formed on the native structure and the T122A mutant. We found that the presence of Thr122 has adeleterious effect on the proton transfer step that is proposed to determine the rate of the reaction.Besides, at the PM3 level, the substitution of Thr122 by Ala does not significantly modify the preferenceof the proton by atom OD2 of Asp76. Transmission coefficients obtained form MP2/6-31G(d,p)//PBE/DZPminimum energy paths show that proton tunneling is significant.