English   español  
Please use this identifier to cite or link to this 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

AuthorsAranda, Carmen; Ullrich, René; Kiebist, Jan; Scheibner, Katrin; Río Andrade, José Carlos del ; Hofrichter, Martin; Martínez, Ángel T. ; Gutiérrez Suárez, Ana
KeywordsAmino acids
Catalytic efficiencies
Chaetomium globosum
Coprinopsis cinerea
Issue Date7-May-2018
PublisherRoyal Society of Chemistry (UK)
CitationCatalysis Science and Technology 8(9): 2394-2401 (2018)
AbstractThis 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.
Description8 páginas.-- 4 figuras.-- 4 tablas.-- 34 referencias.-- Electronic supplementary information (ESI) available. See DOI: 10.1039/c8cy00272j
Publisher version (URL)http://dx.doi.org/10.1039/C8CY00272J
Appears in Collections:(CIB) Artículos
(IRNAS) Artículos
Files in This Item:
File Description SizeFormat 
Selective_synthesis_resveratrol_OA_CC_2018.pdf1,7 MBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.