000075424 001__ 75424
000075424 005__ 20220621094623.0
000075424 0247_ $$2doi$$a10.1039/C7CP05904C
000075424 0248_ $$2sideral$$a102550
000075424 037__ $$aART-2020-102550
000075424 041__ $$aeng
000075424 100__ $$aCarro, Juan
000075424 245__ $$aProtein dynamics promote hydride tunnelling in substrate oxidation by aryl-alcohol oxidase
000075424 260__ $$c2020
000075424 5060_ $$aAccess copy available to the general public$$fUnrestricted
000075424 5203_ $$aThe temperature dependence of hydride transfer from the substrate to the N5 of the FAD cofactor during the reductive half-reaction of Pleurotus eryngii aryl-alcohol oxidase (AAO) is assessed here. Kinetic isotope effects on both the pre-steady state reduction of the enzyme and its steady-state kinetics, with differently deuterated substrates, suggest an environmentally-coupled quantum-mechanical tunnelling process. Moreover, those kinetic data, along with the crystallographic structure of the enzyme in complex with a substrate analogue, indicate that AAO shows a pre-organized active site that would only require the approaching of the hydride donor and acceptor for the tunnelled transfer to take place. Modification of the enzyme''s active-site architecture by replacement of Tyr92, a residue establishing hydrophobic interactions with the substrate analogue in the crystal structure, in the Y92F, Y92L and Y92W variants resulted in different temperature dependence patterns that indicated a role of this residue in modulating the transfer reaction.
000075424 536__ $$9info:eu-repo/grantAgreement/ES/MINECO/NOESIS-BIO2014-56388-R$$9info:eu-repo/grantAgreement/ES/MINECO/BIO2016-75183-P$$9This project has received funding from the European Union’s Horizon 2020 research and innovation program under grant agreement No H2020 720297-EnzOx2$$9info:eu-repo/grantAgreement/EC/H2020/720297/EU/New enzymatic oxidation/oxyfunctionalization technologies for added value bio-based products/EnzOx2$$9info:eu-repo/grantAgreement/EC/FP7/613549/EU/Optimized oxidoreductases for medium and large scale industrial biotransformations/INDOX
000075424 540__ $$9info:eu-repo/semantics/openAccess$$aAll rights reserved$$uhttp://www.europeana.eu/rights/rr-f/
000075424 590__ $$a3.676$$b2020
000075424 591__ $$aPHYSICS, ATOMIC, MOLECULAR & CHEMICAL$$b8 / 37 = 0.216$$c2020$$dQ1$$eT1
000075424 591__ $$aCHEMISTRY, PHYSICAL$$b77 / 162 = 0.475$$c2020$$dQ2$$eT2
000075424 592__ $$a1.052$$b2020
000075424 593__ $$aPhysics and Astronomy (miscellaneous)$$c2020$$dQ1
000075424 593__ $$aPhysical and Theoretical Chemistry$$c2020$$dQ1
000075424 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/acceptedVersion
000075424 700__ $$0(orcid)0000-0001-9047-0046$$aMartínez-Julve, Marta$$uUniversidad de Zaragoza
000075424 700__ $$0(orcid)0000-0001-8743-0182$$aMedina, Milagros$$uUniversidad de Zaragoza
000075424 700__ $$aMartínez, Angel T.
000075424 700__ $$0(orcid)0000-0003-4076-6118$$aFerreira, Patricia$$uUniversidad de Zaragoza
000075424 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000075424 773__ $$g19 (2020), 28666$$pPhys. chem. chem. phys.$$tPhysical Chemistry Chemical Physics$$x1463-9076
000075424 8564_ $$s929175$$uhttps://zaguan.unizar.es/record/75424/files/texto_completo.pdf$$yPostprint
000075424 8564_ $$s111909$$uhttps://zaguan.unizar.es/record/75424/files/texto_completo.jpg?subformat=icon$$xicon$$yPostprint
000075424 909CO $$ooai:zaguan.unizar.es:75424$$particulos$$pdriver
000075424 951__ $$a2022-06-21-09:39:58
000075424 980__ $$aARTICLE