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dc.contributor.authorHosseini, Ali
dc.contributor.authorBrouk, Moran
dc.contributor.authorLucas, Fatima
dc.contributor.authorGlaser, Fabian
dc.contributor.authorFishman, Ayelet
dc.contributor.authorGuallar, Víctor
dc.contributor.otherBarcelona Supercomputing Center
dc.date.accessioned2016-03-14T17:34:16Z
dc.date.available2016-03-14T17:34:16Z
dc.date.issued2014-05-04
dc.identifier.citationHosseini, Ali [et al.]. Atomic picture of ligand migration in toluene 4-monooxygenase. "Journal of Physical Chemistry B", 04 Maig 2014, vol. 119, núm. 3, p. 671-678.
dc.identifier.issn1520-6106
dc.identifier.urihttp://hdl.handle.net/2117/84345
dc.description.abstractComputational modeling combined with mutational and activity assays was used to underline the substrate migration pathways in toluene 4-monooxygenase, a member of the important family of bacterial multicomponent monooxygenases (BMMs). In all structurally defined BMM hydroxylases, several hydrophobic cavities in the α-subunit map a preserved path from the protein surface to the diiron active site. Our results confirm the presence of two pathways by which different aromatic molecules can enter/escape the active site. While the substrate is observed to enter from both channels, the more hydrophilic product is withdrawn mainly from the shorter channel ending at residues D285 and E214. The long channel ends in the vicinity of S395, whose variants have been seen to affect activity and specificity. These mutational effects are clearly reproduced and rationalized by the in silico studies. Furthermore, the combined computational and experimental results highlight the importance of residue F269, which is located at the intersection of the two channels.
dc.description.sponsorshipThis work has been funded by the EU projects INDOX (KBBE20137613549) and ERC 2009Adg25027PELE (to V.G) and the Spanish Ministry of Education and Science project CTQ201348287 (to V.G).
dc.format.extent8 p.
dc.language.isoeng
dc.publisherACS Publications
dc.subjectÀrees temàtiques de la UPC::Enginyeria mecànica::Impacte ambiental
dc.subject.lcshBacteria
dc.subject.lcshMolecules
dc.subject.otherComputational modeling
dc.subject.other4-monooxygenase
dc.subject.otherAromatic molecules
dc.titleAtomic picture of ligand migration in toluene 4-monooxygenase
dc.typeArticle
dc.subject.lemacMolècules
dc.identifier.doi10.1021/jp502509a
dc.description.peerreviewedPeer Reviewed
dc.relation.publisherversionhttp://pubs.acs.org/doi/abs/10.1021/jp502509a
dc.rights.accessOpen Access
dc.description.versionPostprint (author's final draft)
dc.relation.projectidinfo:eu-repo/grantAgreement/EC/FP7/250277/EU/P.E.L.E (Protein Energy Landscape Exploration): a la carte drug design tools/PELE
local.citation.publicationNameJournal of Physical Chemistry B
local.citation.volume119
local.citation.number3
local.citation.startingPage671
local.citation.endingPage678


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