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Title

Protein dynamics promote hydride tunnelling in substrate oxidation by aryl-alcohol oxidase

AuthorsCarro, Juan ; Martínez-Júlvez, Marta; Medina, Milagros; Martínez, Ángel T. CSIC ORCID ; Ferreira, Patricia CSIC ORCID
KeywordsCrystal-structure
Lignin degradation
Catalysis
Pleurotus
Issue Date14-Nov-2017
PublisherRoyal Society of Chemistry (UK)
CitationPhysical Chemistry Chemical Physics 19(42): 28666-28675 (2017)
AbstractThe 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.
Description9 p.-4 fig.-4 tab.
Publisher version (URL)http://dx.doi.org/10.1039/c7cp05904c
URIhttp://hdl.handle.net/10261/161237
DOI10.1039/c7cp05904c
E-ISSN1463-9076
Appears in Collections:(CIB) Artículos

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