The role of residue Thr122 of methylamine dehydrogenase on the proton transfer from the iminoquinone intermediate to residue Asp76

We present the results of combined molecular dynamics and full-quantum calculations aimed at elucidating the role of residue Thr122 of the enzyme methylamine dehydrogenase. Calculations were performed on the native structure and the T122A mutant. We found that the presence of Thr122 has a deleteriou...

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Autores principales: Pierdominici-Sottile, G., Martí, M.A., Palma, J.
Formato: JOUR
Materias:
Amines
Molecular dynamics
Proton transfer
Quantum computers
Reaction rates
Substitution reactions
Enzyme methylamine dehydrogenase
Proton tunneling
Transmission coefficients
Enzyme kinetics
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00092614_v456_n4-6_p243_PierdominiciSottile
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
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spelling todo:paper_00092614_v456_n4-6_p243_PierdominiciSottile2023-10-03T14:08:27Z The role of residue Thr122 of methylamine dehydrogenase on the proton transfer from the iminoquinone intermediate to residue Asp76 Pierdominici-Sottile, G. Martí, M.A. Palma, J. Amines Molecular dynamics Proton transfer Quantum computers Reaction rates Substitution reactions Enzyme methylamine dehydrogenase Proton tunneling Transmission coefficients Enzyme kinetics We present the results of combined molecular dynamics and full-quantum calculations aimed at elucidating the role of residue Thr122 of the enzyme methylamine dehydrogenase. Calculations were performed on the native structure and the T122A mutant. We found that the presence of Thr122 has a deleterious 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 preference of the proton by atom OD2 of Asp76. Transmission coefficients obtained form MP2/6-31G(d,p)//PBE/DZP minimum energy paths show that proton tunneling is significant. © 2008 Elsevier B.V. All rights reserved. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00092614_v456_n4-6_p243_PierdominiciSottile
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Amines
Molecular dynamics
Proton transfer
Quantum computers
Reaction rates
Substitution reactions
Enzyme methylamine dehydrogenase
Proton tunneling
Transmission coefficients
Enzyme kinetics
spellingShingle Amines
Molecular dynamics
Proton transfer
Quantum computers
Reaction rates
Substitution reactions
Enzyme methylamine dehydrogenase
Proton tunneling
Transmission coefficients
Enzyme kinetics
Pierdominici-Sottile, G.
Martí, M.A.
Palma, J.
The role of residue Thr122 of methylamine dehydrogenase on the proton transfer from the iminoquinone intermediate to residue Asp76
topic_facet Amines
Molecular dynamics
Proton transfer
Quantum computers
Reaction rates
Substitution reactions
Enzyme methylamine dehydrogenase
Proton tunneling
Transmission coefficients
Enzyme kinetics
description We present the results of combined molecular dynamics and full-quantum calculations aimed at elucidating the role of residue Thr122 of the enzyme methylamine dehydrogenase. Calculations were performed on the native structure and the T122A mutant. We found that the presence of Thr122 has a deleterious 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 preference of the proton by atom OD2 of Asp76. Transmission coefficients obtained form MP2/6-31G(d,p)//PBE/DZP minimum energy paths show that proton tunneling is significant. © 2008 Elsevier B.V. All rights reserved.
format JOUR
author Pierdominici-Sottile, G.
Martí, M.A.
Palma, J.
author_facet Pierdominici-Sottile, G.
Martí, M.A.
Palma, J.
author_sort Pierdominici-Sottile, G.
title The role of residue Thr122 of methylamine dehydrogenase on the proton transfer from the iminoquinone intermediate to residue Asp76
title_short The role of residue Thr122 of methylamine dehydrogenase on the proton transfer from the iminoquinone intermediate to residue Asp76
title_full The role of residue Thr122 of methylamine dehydrogenase on the proton transfer from the iminoquinone intermediate to residue Asp76
title_fullStr The role of residue Thr122 of methylamine dehydrogenase on the proton transfer from the iminoquinone intermediate to residue Asp76
title_full_unstemmed The role of residue Thr122 of methylamine dehydrogenase on the proton transfer from the iminoquinone intermediate to residue Asp76
title_sort role of residue thr122 of methylamine dehydrogenase on the proton transfer from the iminoquinone intermediate to residue asp76
url http://hdl.handle.net/20.500.12110/paper_00092614_v456_n4-6_p243_PierdominiciSottile
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