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OXIDATION OF DIBENZOTHIOPHENE CATALYZED BY HEMOGLOBIN AND OTHER HEMOPROTEINS IN VARIOUS AQUEOUS-ORGANIC MEDIAстатья
Информация о цитировании статьи получена из
Scopus,
Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: KLYACHKO NL, KLIBANOV AM
- Журнал: Applied Biochemistry and Biotechnology
- Том: 37
- Номер: 1
- Год издания: 1992
- Издательство: Humana Press, Inc.
- Местоположение издательства: United States
- Первая страница: 53
- Последняя страница: 68
- DOI: 10.1007/BF02788857
- Аннотация: Biocatalytic oxidation of dibenzothiophene (a model of organic sulfur in coal) with hydrogen peroxide was investigated. it was found that various hemoproteins, both enzymic (e.g., horseradish peroxidase) and nonenzymic (e.g., bovine blood hemoglobin), readily oxidized dibensothiophene to its S-oxide and, to a minor extent, further to its S-dioxide (sulfone). This process catalyzed by hemoglobin (a slaughter-house waste protein) was studied in a number of monophasic aqueous-organic mixtures. Although hemoglobin was competent as an oxidation catalyst even in nearly dry organic solvents (with protic, acidic solvents being optimal), the highest conversions were observed in predominantly aqueous media. The hemoglobin-catalyzed oxidation of dibenzothiophene at low concentrations of the protein stopped long before all the substrate was oxidized. This phenomenon was caused by inactivation of hemoglobin by hydrogen peroxide that destroyed the heme moiety. The maximal degree of the hemoglobin-catalyzed dibenzothiophene oxidation was predicted, and found, to be strongly dependent on the reaction medium composition.
- Добавил в систему: Клячко Наталья Львовна