INSTITUTO DE QUIMICA, FISICA DE LOS MATERIALES, MEDIOAMBIENTE Y ENERGIA
Unidad Ejecutora - UE
The role of residue Thr122 of methylamine dehydrogenase on the proton transfer from the iminoquinone intermediate to residue Asp76
GUSTAVO PIERDOMINICI-SOTTILE; MARCELO A. MARTI; JULIANA PALMA
CHEMICAL PHYSICS LETTERS
Año: 2008 p. 243 - 243
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.