Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase

This is the peer reviewed version of the following article: [Ferreira, P., Hernández-Ortega, A., Lucas, F., Carro, J., Herguedas, B., Borrelli, K. W., Guallar, V., Martínez, A. T. and Medina, M. (2015), Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase. FEBS J, 282: 3091–3106....

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Autores: Ferreira, Patricia, Hernández-Ortega, Aitor, Lucas, Fatima, Carro, Juan, Herguedas, Beatriz, Borrelli, Kenneth W., Guallar, Víctor|||0000-0002-4580-1114, Martínez, Angel T., Medina, Milagros
Tipo de recurso: artículo
Fecha de publicación:2015
País:España
Institución:Universitat Politècnica de Catalunya (UPC)
Repositorio:UPCommons. Portal del coneixement obert de la UPC
Idioma:inglés
OAI Identifier:oai:upcommons.upc.edu:2117/84358
Acceso en línea:https://hdl.handle.net/2117/84358
https://dx.doi.org/10.1111/febs.13221
Access Level:acceso abierto
Palabra clave:Oxidation--Measurement
Catalysis
Aryl-alcohol oxidase
GMC oxidoreductases
Aromatic stacking
Catalytic mechanism
Ternary complex
Charge-transfer complexes
Kinetic isotope effect
Steady-state kinetics
Pre-steady-state kinetics
Oxidació
Àrees temàtiques de la UPC::Enginyeria mecànica::Impacte ambiental
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oai_identifier_str oai:upcommons.upc.edu:2117/84358
network_acronym_str ES
network_name_str España
repository_id_str
dc.title.none.fl_str_mv Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase
Substrate stacking interactions in aryl-alcohol oxidase
title Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase
spellingShingle Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase
Ferreira, Patricia
Oxidation--Measurement
Catalysis
Aryl-alcohol oxidase
GMC oxidoreductases
Aromatic stacking
Catalytic mechanism
Ternary complex
Charge-transfer complexes
Kinetic isotope effect
Steady-state kinetics
Pre-steady-state kinetics
Oxidació
Àrees temàtiques de la UPC::Enginyeria mecànica::Impacte ambiental
title_short Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase
title_full Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase
title_fullStr Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase
title_full_unstemmed Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase
title_sort Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase
dc.creator.none.fl_str_mv Ferreira, Patricia
Hernández-Ortega, Aitor
Lucas, Fatima
Carro, Juan
Herguedas, Beatriz
Borrelli, Kenneth W.
Guallar, Víctor|||0000-0002-4580-1114
Martínez, Angel T.
Medina, Milagros
author Ferreira, Patricia
author_facet Ferreira, Patricia
Hernández-Ortega, Aitor
Lucas, Fatima
Carro, Juan
Herguedas, Beatriz
Borrelli, Kenneth W.
Guallar, Víctor|||0000-0002-4580-1114
Martínez, Angel T.
Medina, Milagros
author_role author
author2 Hernández-Ortega, Aitor
Lucas, Fatima
Carro, Juan
Herguedas, Beatriz
Borrelli, Kenneth W.
Guallar, Víctor|||0000-0002-4580-1114
Martínez, Angel T.
Medina, Milagros
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Oxidation--Measurement
Catalysis
Aryl-alcohol oxidase
GMC oxidoreductases
Aromatic stacking
Catalytic mechanism
Ternary complex
Charge-transfer complexes
Kinetic isotope effect
Steady-state kinetics
Pre-steady-state kinetics
Oxidació
Àrees temàtiques de la UPC::Enginyeria mecànica::Impacte ambiental
topic Oxidation--Measurement
Catalysis
Aryl-alcohol oxidase
GMC oxidoreductases
Aromatic stacking
Catalytic mechanism
Ternary complex
Charge-transfer complexes
Kinetic isotope effect
Steady-state kinetics
Pre-steady-state kinetics
Oxidació
Àrees temàtiques de la UPC::Enginyeria mecànica::Impacte ambiental
description This is the peer reviewed version of the following article: [Ferreira, P., Hernández-Ortega, A., Lucas, F., Carro, J., Herguedas, B., Borrelli, K. W., Guallar, V., Martínez, A. T. and Medina, M. (2015), Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase. FEBS J, 282: 3091–3106. doi:10.1111/febs.13221], which has been published in final form at [10.1111/febs.13221]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving." http://olabout.wiley.com/WileyCDA/Section/id-820227.html The version posted may not be updated or replaced with the final published version (the Version of Record).
publishDate 2015
dc.date.none.fl_str_mv 2015
2015-02-23
2016
2016-03-15
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
AM
http://purl.org/coar/version/c_ab4af688f83e57aa
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/2117/84358
https://dx.doi.org/10.1111/febs.13221
url https://hdl.handle.net/2117/84358
https://dx.doi.org/10.1111/febs.13221
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.relation.none.fl_str_mv Ministerio de Economía y Competitividad http://doi.org/10.13039/501100003329 BIO2013-42978-P SISTEMAS DEPENDIENTES DE FLAVOENZIMAS: DE SUS MECANISMOS DE ACCION A SUS APLICACIONES BIOTECNOLOGICAS Y SANITARIAS
Ministerio de Ciencia e Innovación http://doi.org/10.13039/501100004837 BIO2011-26694 BUSQUEDA E INGENIERIA DE NUEVAS PEROXIDASAS FUNGICAS DE ALTO POTENCIAL REDOX
Ministerio de Ciencia e Innovación http://doi.org/10.13039/501100004837 CTQ2010-18123 QM%2FMM E-PATHWAY: ESTUDIO DE TRANSFERENCIAS ELECTRONICAS DE LARGO ALCANCE.
European Commission http://dx.doi.org/10.13039/100011102 Seventh Framework Programme 613549 Optimized oxidoreductases for medium and large scale industrial biotransformations
European Commission http://dx.doi.org/10.13039/100011102 Seventh Framework Programme 250277 P.E.L.E (Protein Energy Landscape Exploration): a la carte drug design tools
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv FEBSPress
publisher.none.fl_str_mv FEBSPress
dc.source.none.fl_str_mv reponame:UPCommons. Portal del coneixement obert de la UPC
instname:Universitat Politècnica de Catalunya (UPC)
instname_str Universitat Politècnica de Catalunya (UPC)
reponame_str UPCommons. Portal del coneixement obert de la UPC
collection UPCommons. Portal del coneixement obert de la UPC
repository.name.fl_str_mv
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spelling Aromatic stacking interactions govern catalysis in aryl-alcohol oxidaseSubstrate stacking interactions in aryl-alcohol oxidaseFerreira, PatriciaHernández-Ortega, AitorLucas, FatimaCarro, JuanHerguedas, BeatrizBorrelli, Kenneth W.Guallar, Víctor|||0000-0002-4580-1114Martínez, Angel T.Medina, MilagrosOxidation--MeasurementCatalysisAryl-alcohol oxidaseGMC oxidoreductasesAromatic stackingCatalytic mechanismTernary complexCharge-transfer complexesKinetic isotope effectSteady-state kineticsPre-steady-state kineticsOxidacióÀrees temàtiques de la UPC::Enginyeria mecànica::Impacte ambientalThis is the peer reviewed version of the following article: [Ferreira, P., Hernández-Ortega, A., Lucas, F., Carro, J., Herguedas, B., Borrelli, K. W., Guallar, V., Martínez, A. T. and Medina, M. (2015), Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase. FEBS J, 282: 3091–3106. doi:10.1111/febs.13221], which has been published in final form at [10.1111/febs.13221]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving." http://olabout.wiley.com/WileyCDA/Section/id-820227.html The version posted may not be updated or replaced with the final published version (the Version of Record).Aryl-alcohol oxidase (AAO, EC 1.1.3.7) generates H2O2 for lignin degradation at the expense of benzylic and other π system-containing primary alcohols, which are oxidized to the corresponding aldehydes. Ligand diffusion studies on Pleurotus eryngii AAO showed a T-shaped stacking interaction between the Tyr92 side chain and the alcohol substrate at the catalytically competent position for concerted hydride and proton transfers. Bi-substrate kinetics analysis revealed that reactions with 3-chloro- or 3-fluorobenzyl alcohols (halogen substituents) proceed via a ping–pong mechanism. However, mono- and dimethoxylated substituents (in 4-methoxybenzyl and 3,4-dimethoxybenzyl alcohols) altered the mechanism and a ternary complex was formed. Electron-withdrawing substituents resulted in lower quantum mechanics stacking energies between aldehyde and the tyrosine side chain, contributing to product release, in agreement with the ping–pong mechanism observed in 3-chloro- and 3-fluorobenzyl alcohol kinetics analysis. In contrast, the higher stacking energies when electron donor substituents are present result in reaction of O2 with the flavin through a ternary complex, in agreement with the kinetics of methoxylated alcohols. The contribution of Tyr92 to the AAO reaction mechanism was investigated by calculation of stacking interaction energies and site-directed mutagenesis. Replacement of Tyr92 by phenylalanine does not alter the AAO kinetic constants (on 4-methoxybenzyl alcohol), most probably because the stacking interaction is still possible. However, introduction of a tryptophan residue at this position strongly reduced the affinity for the substrate (i.e. the pre-steady state Kd and steady-state Km increase by 150-fold and 75-fold, respectively), and therefore the steady-state catalytic efficiency, suggesting that proper stacking is impossible with this bulky residue. The above results confirm the role of Tyr92 in substrate binding, thus governing the kinetic mechanism in AAO.This work was supported by the BIO2013-42978-P (to MM), BIO2011-26694 (to ATM), “Juan de la Cierva” (to FL) and CTQ2010-18123 (to VG) Grants of the Spanish Ministry of Economy and Competitiveness (MINECO) and by the INDOX (KBBE-2013-7-613549, to ATM) and PELE (ERC-2009-Adg 25027, to VG) European projects.Peer ReviewedFEBSPress20152015-02-2320162016-03-15journal articlehttp://purl.org/coar/resource_type/c_6501AMhttp://purl.org/coar/version/c_ab4af688f83e57aainfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/2117/84358https://dx.doi.org/10.1111/febs.13221reponame:UPCommons. Portal del coneixement obert de la UPCinstname:Universitat Politècnica de Catalunya (UPC)InglésengMinisterio de Economía y Competitividad http://doi.org/10.13039/501100003329 BIO2013-42978-P SISTEMAS DEPENDIENTES DE FLAVOENZIMAS: DE SUS MECANISMOS DE ACCION A SUS APLICACIONES BIOTECNOLOGICAS Y SANITARIASMinisterio de Ciencia e Innovación http://doi.org/10.13039/501100004837 BIO2011-26694 BUSQUEDA E INGENIERIA DE NUEVAS PEROXIDASAS FUNGICAS DE ALTO POTENCIAL REDOXMinisterio de Ciencia e Innovación http://doi.org/10.13039/501100004837 CTQ2010-18123 QM%2FMM E-PATHWAY: ESTUDIO DE TRANSFERENCIAS ELECTRONICAS DE LARGO ALCANCE.European Commission http://dx.doi.org/10.13039/100011102 Seventh Framework Programme 613549 Optimized oxidoreductases for medium and large scale industrial biotransformationsEuropean Commission http://dx.doi.org/10.13039/100011102 Seventh Framework Programme 250277 P.E.L.E (Protein Energy Landscape Exploration): a la carte drug design toolsopen accesshttp://purl.org/coar/access_right/c_abf2info:eu-repo/semantics/openAccessoai:upcommons.upc.edu:2117/843582026-05-27T15:37:01Z
score 15,198674

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