Hemoglobin,horseradish peroxidase,and heme-bovine serum albumin as biocatalyst for the oxidation of dibenzothiophene |
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Authors: | Thérèse Stachyra Didier Guillochom Sylviane Pulvin Daniel Thomas |
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Affiliation: | (1) Laboratoire de Technologie Enzymatique, Unité de recherche associée 1442 du Centre National de La Recherche Scientifique, Université de Technologie de Compiegne, BP 649-60206, Compiegne Cédex, France;(2) Laboratoire de Technologie des Substances Naturelles, Villeneuve d’Ascq Cédex, France |
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Abstract: | Hemoglobin, horseradish peroxidase, and bovine serum albumin incubated heme-catalyzed the oxidation of dibenzothiophene into sulfoxide in the presence of hydrogen peroxide. This reaction was carried out in an aqueous buffer containing 25% of water-miscible organic solvents. The observation of this transient state of hemoproteins during sulfoxidation showed heme degradation. None of the compounds usually involved in a classical peroxidative activity mechanism were detected. Furthermore, this activity did not appear to be based on a Fenton-type reaction. The highest degrees of sulfoxidation were obtained with hemoglobin. Under the best conditions of reaction, 100% of dibenzothiophene were converted into dibenzothiophene sulfoxide by hemoglobin. Heat-denatured hemoproteins did keep their sulfoxidation activity. With hemoglobin, a kcat of 0.22 min-1 was determined. Nearly the same values were obtained with heat-denatured hemoglobin and bovine serum albumin-adsorbed heme. With horseradish peroxidase, only 4% of conversion was attained. This percentage could be slightly increased by using a less pure peroxidase or heat-denatured peroxidase. |
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Keywords: | Hemoglobin peroxidase heme-BSA dibenzothiophene heat-denatured hemoprotein heme-dependent oxidation aqueous-organic media peroxidase activity reactive oxygen species |
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