English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/165155
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

Selective synthesis of the resveratrol analogue 4,4′-dihydroxy-: Trans -stilbene and stilbenoids modification by fungal peroxygenases

AutorAranda, Carmen; Ullrich, René; Kiebist, Jan; Scheibner, Katrin; Río Andrade, José Carlos del ; Hofrichter, Martin; Martínez, Ángel T. ; Gutiérrez Suárez, Ana
Palabras claveAmino acids
Catalytic efficiencies
Chaetomium globosum
Coprinopsis cinerea
Fecha de publicación7-may-2018
EditorRoyal Society of Chemistry (Great Britain)
CitaciónCatalysis Science and Technology 8(9): 2394-2401 (2018)
ResumenThis work gives first evidence that the unspecific peroxygenases (UPOs) from the basidiomycetes Agrocybe aegerita (AaeUPO), Coprinopsis cinerea (rCciUPO) and Marasmius rotula (MroUPO) are able to catalyze the regioselective hydroxylation of trans-stilbene to 4,4′-dihydroxy-trans-stilbene (DHS), a resveratrol (RSV) analogue whose preventive effects on cancer invasion and metastasis have very recently been shown. Nearly complete transformation of substrate (yielding DHS) was achieved with the three enzymes tested, using H2O2 as the only co-substrate, with AaeUPO showing exceptionally higher total turnover number (200000) than MroUPO (26000) and rCciUPO (1400). Kinetic studies demonstrated that AaeUPO was the most efficient enzyme catalyzing stilbene dihydroxylation with catalytic efficiencies (kcat/Km) one and two orders of magnitude higher than those of MroUPO and rCciUPO, so that 4-hydroxystilbene appears to be the best UPO substrate reported to date. In contrast, the peroxygenase from the ascomycete Chaetomium globosum (CglUPO) failed to hydroxylate trans-stilbene at the aromatic ring and instead produced the trans-epoxide in the alkenyl moiety. In addition, stilbenoids such as pinosylvin (Pin) and RSV were tested as substrates for the enzymatic synthesis of RSV from Pin and oxyresveratrol (oxyRSV) from both RSV and Pin. Overall, lower conversion rates and regioselectivities compared with trans-stilbene were accomplished by three of the UPOs, and no conversion was observed with CglUPO. The highest amount of RSV (63% of products) and oxyRSV (78%) were again attained with AaeUPO. True peroxygenase activity was demonstrated by incorporation of 18O from H218O2 into the stilbene hydroxylation products. Differences in the number of phenylalanine residues at the heme access channels seems related to differences in aromatic hydroxylation activity, since they would facilitate substrate positioning by aromatic-aromatic interactions. The only ascomycete UPO tested (that of C. globosum) turned out to have the most differing active site (distal side of heme cavity) and reactivity with stilbenes resulting in ethenyl epoxidation instead of aromatic hydroxylation. The above oxyfunctionalizations by fungal UPOs represent a novel and simple alternative to chemical synthesis for the production of DHS, RSV and oxyRSV.
Descripción8 páginas.-- 4 figuras.-- 4 tablas.-- 34 referencias.-- Electronic supplementary information (ESI) available. See DOI: 10.1039/c8cy00272j
Versión del editorhttp://dx.doi.org/10.1039/C8CY00272J
Aparece en las colecciones: (CIB) Artículos
(IRNAS) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
Selective_synthesis_resveratrol_OA_CC_2018.pdf1,7 MBAdobe PDFVista previa
Mostrar el registro completo

NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.