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Linking electrostatic effects and protein motions in enzymatic catalysis. A theoretical analysis of catechol o-methyltransferase

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Linking electrostatic effects and protein motions in enzymatic catalysis. A theoretical analysis of catechol o-methyltransferase

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dc.contributor.author	García Meseguer, Rafael
dc.contributor.author	Zinovjev, Kirill
dc.contributor.author	Roca Moliner, María Teresa
dc.contributor.author	Ruiz Pernía, José Javier
dc.contributor.author	Tuñón, Iñaki
dc.date.accessioned	2015-04-21T12:05:23Z
dc.date.available	2015-08-27T03:45:06Z
dc.date.issued	2014
dc.identifier.citation	García Meseguer, Rafael Zinovjev, Kirill Roca Moliner, María Teresa Ruiz Pernía, José Javier Tuñón García de Vicuña, Ignacio 2014 Linking electrostatic effects and protein motions in enzymatic catalysis. A theoretical analysis of catechol o-methyltransferase Journal of Physical Chemistry B 119 3 873 882
dc.identifier.uri	http://hdl.handle.net/10550/43258
dc.description.abstract	The role of protein motions in enzymatic catalysis is the subject of a hot scientific debate. We here propose the use of an explicit solvent coordinate to analyze the impact of environmental motions during the reaction process. The example analyzed here is the reaction catalyzed by catechol O-methyltransferase, a methyl transfer reaction from S-adenosylmethionine (SAM) to the nucleophilic oxygen atom of catecholate. This reaction proceeds from a charged reactant to a neutral product, and then a large electrostatic coupling with the environment could be expected. By means of a two-dimensional free energy surface, we show that a large fraction of the environmental motions needed to attain the transition state happens during the first stages of the reaction because most of the environmental motions are slower than changes in the substrate. The incorporation of the solvent coordinate in the definition of the transition state improves the transmission coefficient and the committor histogram in solution, while the changes are much less significant in the enzyme. The equilibrium solvation approach seems then to work better in the enzyme than in aqueous solution because the enzyme provides a preorganized environment where the reaction takes place.
dc.language.iso	eng
dc.relation.ispartof	Journal of Physical Chemistry B, 2014, vol. 119, num. 3, p. 873-882
dc.subject	Fisicoquímica
dc.subject	Proteïnes
dc.title	Linking electrostatic effects and protein motions in enzymatic catalysis. A theoretical analysis of catechol o-methyltransferase
dc.type	journal article	es_ES
dc.date.updated	2015-04-21T12:05:23Z
dc.identifier.doi	10.1021/jp505746x
dc.identifier.idgrec	099382
dc.embargo.terms	1 year
dc.rights.accessRights	open access	es_ES