The thermostable truncated hemoglobin from the actinomyces Thermobifida fusca (Tf-trHb) displays a robust peroxidase activity, with optimum at acidic pH values, in experiments with the redox mediator ABTS. However, typical peroxidase substrates, such as phenolic or aromatic amine compounds. appear to be poor substrates for Tf-trHb. In turn, the protein is able to catalyze a unique dehydrogenation reaction of dibenzylbutanolides, suggested intermediates in the biosynthesis of podophyllotoxin, in the presence of hydrogen peroxide. Dibenzylbutanolides with a free 4 ''-hydroxyl group were thus converted into the corresponding 2,7 ''-dehydroderivatives thus setting up the basis for an efficient biotransformation of this important precursor. In particular, Tf-trHb mediated oxidation of trans-2-(4 ''-hydroxy-3 '',5 ''-dimethoxybenzyl)-3-(3',4'-methylenedioxy-7'beta-hydroxybenzyl)butanolide 1 into the corresponding benzylidene-benzoyl-gamma-butyrolactone 2 was obtained at high yield and with excellent selectivity. (C) 2009 Elsevier B.V. All rights reserved.

Peroxidase-like activity of Thermobifida fusca hemoglobin: The oxidation of dibenzylbutanolide / Torge, Roberta; Alessandra, Comandini; Bruno, Catacchio; Bonamore, Alessandra; Botta, Bruno; Boffi, Alberto. - In: JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC. - ISSN 1381-1177. - STAMPA. - 61:3-4(2009), pp. 303-308. [10.1016/j.molcatb.2009.08.010]

Peroxidase-like activity of Thermobifida fusca hemoglobin: The oxidation of dibenzylbutanolide

TORGE, ROBERTA;BONAMORE, ALESSANDRA;BOTTA, Bruno;BOFFI, Alberto
2009

Abstract

The thermostable truncated hemoglobin from the actinomyces Thermobifida fusca (Tf-trHb) displays a robust peroxidase activity, with optimum at acidic pH values, in experiments with the redox mediator ABTS. However, typical peroxidase substrates, such as phenolic or aromatic amine compounds. appear to be poor substrates for Tf-trHb. In turn, the protein is able to catalyze a unique dehydrogenation reaction of dibenzylbutanolides, suggested intermediates in the biosynthesis of podophyllotoxin, in the presence of hydrogen peroxide. Dibenzylbutanolides with a free 4 ''-hydroxyl group were thus converted into the corresponding 2,7 ''-dehydroderivatives thus setting up the basis for an efficient biotransformation of this important precursor. In particular, Tf-trHb mediated oxidation of trans-2-(4 ''-hydroxy-3 '',5 ''-dimethoxybenzyl)-3-(3',4'-methylenedioxy-7'beta-hydroxybenzyl)butanolide 1 into the corresponding benzylidene-benzoyl-gamma-butyrolactone 2 was obtained at high yield and with excellent selectivity. (C) 2009 Elsevier B.V. All rights reserved.
2009
dehydrogenation; dibenzylbutanolides; etoposide; thermobifida fusca; truncated hemoglobin
01 Pubblicazione su rivista::01a Articolo in rivista
Peroxidase-like activity of Thermobifida fusca hemoglobin: The oxidation of dibenzylbutanolide / Torge, Roberta; Alessandra, Comandini; Bruno, Catacchio; Bonamore, Alessandra; Botta, Bruno; Boffi, Alberto. - In: JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC. - ISSN 1381-1177. - STAMPA. - 61:3-4(2009), pp. 303-308. [10.1016/j.molcatb.2009.08.010]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/360869
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