Mostra el registre d'ítem simple

dc.contributor.authorRobert, Viviane
dc.contributor.authorMonza, Emanuele
dc.contributor.authorTarrago, Lionel
dc.contributor.authorSancho, Ferran
dc.contributor.authorde Falco, Ana
dc.contributor.authorSchneider, Ludovic
dc.contributor.authorNgoutane, Eloïne N.
dc.contributor.authorMekmouche, Yasmina
dc.contributor.authorPailley, Pierre R.
dc.contributor.authorSimaan, A. Jalila
dc.contributor.authorGuallar, Victor
dc.contributor.authorTron, Thierry
dc.contributor.otherBarcelona Supercomputing Center
dc.date.accessioned2017-05-19T10:30:51Z
dc.date.available2017-05-19T10:30:51Z
dc.date.issued2017-04
dc.identifier.citationRobert, V. [et al.]. Probing the Surface of a Laccase for Clues towards the Design of Chemo-Enzymatic Catalysts. "ChemPlusChem", Abril 2017, vol. 82, núm. 4, p. 607-614.
dc.identifier.issn2192-6506
dc.identifier.urihttp://hdl.handle.net/2117/104643
dc.description.abstractSystems featuring a multi-copper oxidase associated with transition-metal complexes can be used to perform oxidation reactions in mild conditions. Here, a strategy is presented for achieving a controlled orientation of a ruthenium–polypyridyl graft at the surface of a fungal laccase. Laccase variants are engineered with unique surface-accessible lysine residues. Distinct ruthenium–polypyridyl-modified laccases are obtained by the reductive alkylation of lysine residues precisely located relative to the T1 copper centre of the enzyme. In none of these hybrids does the presence of the graft compromise the catalytic efficiency of the enzyme on the substrate 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid). Furthermore, the efficiency of the hybrids in olefin oxidation coupled to the light-driven reduction of O2 is highly dependent on the location of the graft at the enzyme surface. Simulated RuII–CuII electron coupling values and distances fit well the observed reactivity and could be used to guide future hybrid designs.
dc.description.sponsorshipL.S. was the recipient of a MinistHre de l’Education Nationale fellowship. This study was supported by grants from the Agence Nationale de la Recherche (ANR-09-BLANC-0176 and ANR-15-CE07-0021-01) and from the Ministerio de EconomÍa, Industria y Competitividad (CTQ2016-79138-R). We thank Elise Courvoisier-Dezord from the Plateforme AVB (AMU): Analyse et Valorisation de la Biodiversit8 and Yolande Charmasson for help in the production of the recombinant enzymes, as well as Pascal Mansuelle and R8gine Lebrun from the Plateforme Prot8omique (CNRSAMU) for help in acquiring mass spectrometry data.
dc.format.extent8 p.
dc.language.isoeng
dc.publisherWiley
dc.subjectÀrees temàtiques de la UPC::Enginyeria biomèdica
dc.subject.lcshEnzyme complexes
dc.subject.lcshProtein interactions
dc.subject.otherChemo-Enzymatic Catalysts
dc.subject.otherLacasse variants
dc.subject.otherEnzyme
dc.titleProbing the Surface of a Laccase for Clues towards the Design of Chemo-Enzymatic Catalysts
dc.typeArticle
dc.subject.lemacProteïnes--Anàlisi
dc.subject.lemacEnzims
dc.identifier.doi10.1002/cplu.201700030
dc.description.peerreviewedPeer Reviewed
dc.relation.publisherversionhttp://onlinelibrary.wiley.com/doi/10.1002/cplu.201700030/abstract
dc.rights.accessOpen Access
dc.description.versionPostprint (published version)
dc.relation.projectidinfo:eu-repo/grantAgreement/MINECO/1PE/CTQ2016-79138-R
local.citation.publicationNameChemPlusChem
local.citation.volume82
local.citation.number4
local.citation.startingPage607
local.citation.endingPage614


Fitxers d'aquest items

Thumbnail

Aquest ítem apareix a les col·leccions següents

Mostra el registre d'ítem simple