http://www.cnr.it/ontology/cnr/individuo/prodotto/ID33430
Chemical Messengers: Mediated Oxidations with the Enzyme Laccase (Articolo in rivista)
- Type
- Label
- Chemical Messengers: Mediated Oxidations with the Enzyme Laccase (Articolo in rivista) (literal)
- Anno
- 2004-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/poc.812 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Galli C. , Gentili P. (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Dipartimento di Chimica, Universita` 'La Sapienza', and IMC-CNR Sezione Meccanismi di Reazione (literal)
- Titolo
- Chemical Messengers: Mediated Oxidations with the Enzyme Laccase (literal)
- Abstract
- The use of low molecular-weight compounds (viz., mediators) in combination with fungal laccase
makes the enzyme suitable for the oxidation of 'non-natural' non-phenolic substrates. Benzyl alcohols are thus
oxidised to carbonylic products by laccase/mediator systems in the presence of oxygen, although laccase cannot
oxidise these substrates directly. The reaction is carried out by the oxidised form of the mediator (Medox), generated
on its interaction with laccase, and the structure of the Medox species is crucial for the mechanism of the ensuing nonenzymatic
oxidation of the substrate. 1-Hydroxybenzotriazole (HBT), N-hydroxyphthalimide (HPI), violuric acid
(VLA) and TEMPO have been investigated as mediators, and experimental evidence is provided that enables the
radical hydrogen atom transfer route with the laccase/HBT, laccase/HPI and laccase/VLA systems to be assessed
unambiguously, although the laccase/TEMPO system follows a different and ionic oxidation route. (literal)
- Prodotto di
- Autore CNR
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
