Substrate and Inhibitor Spectra of Ethylbenzene Dehydrogenase: Perspectives on Application Potential and Catalytic Mechanism
dc.contributor.author | Knack, Daniel | |
dc.contributor.author | Hagel, Corina | |
dc.contributor.author | Szaleniec, Maciej | |
dc.contributor.author | Dudzik, Agnieszka | |
dc.contributor.author | Salwinski, Aleksander | |
dc.contributor.author | Heidera, Johann | |
dc.date.accessioned | 2017-03-02T08:32:04Z | |
dc.date.available | 2017-03-02T08:32:04Z | |
dc.date.issued | 2012-06-06 | |
dc.identifier.citation | D. Knack, C. Hagel, M. Szaleniec, A. Dudzik, A. Salwinski, J. Heider, "Substrate and inhibitor spectrum of ethylbenzene dehydrogenase: perspectives on application potential and catalytic mechanism", Appl. Environ. Microb., 78 (2012) 6475–6482 | pl_PL |
dc.identifier.issn | 0099-2240 | |
dc.identifier.uri | https://depot.ceon.pl/handle/123456789/11631 | |
dc.description.abstract | Ethylbenzene dehydrogenase (EbDH) catalyzes the initial step in anaerobic degradation of ethylbenzene in denitrifying bacteria, namely, the oxygen-independent hydroxylation of ethylbenzene to (S)-1-phenylethanol. In our study we investigate the kinetic properties of 46 substrate analogs acting as substrates or inhibitors of the enzyme. The apparent kinetic parameters of these compounds give important insights into the function of the enzyme and are consistent with the predicted catalytic mechanism based on a quantum chemical calculation model. In particular, the existence of the proposed substrate-derived radical and carbocation intermediates is substantiated by the formation of alternative dehydrogenated and hydroxylated products from some substrates, which can be regarded as mechanistic models. In addition, these results also show the surprisingly high diversity of EbDH in hydroxylating different kinds of alkylaromatic and heterocyclic compounds to the respective alcohols. This may lead to attractive industrial applications of ethylbenzene dehydrogenase for a new process of producing alcohols via hydroxylation of the corresponding aromatic hydrocarbons rather than the customary procedure of reducing the corresponding ketones. | pl_PL |
dc.description.sponsorship | the priority program 1319 of the German Research Foundation (DFG), he excellence program LOEWE/Synmikro from the state of Hessen in Germany, computational grant MNiSW/SGI3700/PAN/121/2006, the Polish National Science Center under grant N N204 269038, Biotransformations for Pharmaceutical and Cosmetics Industry No. POIG.01.03.01-00-158/09-00, funded in part by the European Union within the European Regional Development Fund. | pl_PL |
dc.publisher | American Society for Microbiology | pl_PL |
dc.rights | Dozwolony użytek | |
dc.subject | molybdenum enzyme | pl_PL |
dc.subject | ethylbenzne dehydrogenase | pl_PL |
dc.title | Substrate and Inhibitor Spectra of Ethylbenzene Dehydrogenase: Perspectives on Application Potential and Catalytic Mechanism | pl_PL |
dc.type | info:eu-repo/semantics/article | pl_PL |
dc.contributor.organization | Laboratory for Microbial Biochemistry, Philipps University of Marburg, Germany | pl_PL |
dc.contributor.organization | Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences | pl_PL |
dc.description.eperson | Maciej Szaleniec |
Pliki tej pozycji
Pozycja umieszczona jest w następujących kolekcjach
-
Artykuły / Articles [16158]
Korzystanie z tego materiału jest możliwe zgodnie z właściwymi przepisami o dozwolonym użytku lub o innych wyjątkach przewidzianych w przepisach prawa, a korzystanie w szerszym zakresie wymaga uzyskania zgody uprawnionego.