An Assessment of the Realative Contributions of Redoc and Steric Issue to Laccase Specificità Towards Substrates (Articolo in rivista)

Type
Label
  • An Assessment of the Realative Contributions of Redoc and Steric Issue to Laccase Specificità Towards Substrates (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1039/b716002j (literal)
Alternative label
  • Aweke Tadesse M.; D'’Annibale A.; Galli C.; Gentili P.; Sergi F. (2008)
    An Assessment of the Realative Contributions of Redoc and Steric Issue to Laccase Specificità Towards Substrates
    in Organic & biomolecular chemistry
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Aweke Tadesse M.; D'’Annibale A.; Galli C.; Gentili P.; Sergi F. (literal)
Pagina inizio
  • 868 (literal)
Pagina fine
  • 878 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 6 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Dipartimento diChimica, Universit`a 'La Sapienza', and IMC-CNR Sezione Meccanismi di Reazione (literal)
Titolo
  • An Assessment of the Realative Contributions of Redoc and Steric Issue to Laccase Specificità Towards Substrates (literal)
Abstract
  • Laccases catalyze the one-electron oxidation of a broad range of substrates coupled to the 4 electron reduction of O2 to H2O. Phenols are typical substrates, because their redox potentials (ranging from 0.5 to 1.0 V vs. NHE) are low enough to allow electron abstraction by the T1 Cu(II) that, although a relatively modest oxidant (in the 0.4-0.8 V range), is the electron-acceptor in laccases. The present study comparatively investigated the oxidation performances of Trametes villosa and Myceliophthora thermophila laccases, two enzymes markedly differing in redox potential (0.79 and 0.46 V). The oxidation efficiency and kinetic constants of laccase-catalyzed conversion of putative substrates were determined. Hammett plots related to the oxidation of substituted phenols by the two laccases, in combination with the kinetic isotope effect determination, confirmed a rate-determining electron transfer from the substrate to the enzyme. The efficiency of oxidation was found to increase with the decrease in redox potential of the substrates, and theMarcus reorganisation energy for electron transfer to the T1 copper site was determined. Steric hindrance to substrate docking was inferred because some of the phenols and anilines investigated, despite possessing a redox potential compatible with one-electron abstraction, were scarcely oxidised. A threshold value of steric hindrance of the substrate, allowed for fitting into the active site of T. villosa laccase, was extrapolated from structural information provided by X-ray analysis of T. versicolor lac3B, sharing an identity of 99% at the protein level, thus enabling us to assess the relative contribution of steric and redox properties of a substrate in determining its susceptibility to laccase oxidation. The inferred structural threshold is compatible with the distance between two phenylalanine residues that mark the entrance to the active site. Interaction of the substrate with other residues of the active site is commented on. (literal)
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