期刊
JOURNAL OF MOLECULAR MICROBIOLOGY AND BIOTECHNOLOGY
卷 26, 期 1-3, 页码 45-62出版社
KARGER
DOI: 10.1159/000441357
关键词
Ethylbenzene dehydrogenase; Cholesterol C25 hydroxylase; p-Cymene hydroxylation; Molybdenum enzyme; Alkane hydroxylation; Anaerobic degradation
资金
- Deutsche Forschungsgemeinschaft (Priority Programme 1319)
- state of Hessen (via the LOEWE Center for Synthetic Microbiology)
- Polish National Center of Research and Development [LIDER/33/147/L-3/11/NCBR]
- Polish National Center of Science [2012/05/D/ST4/00277]
- project 'Biotransformations for pharmaceutical and cosmetic industry' [POIG.01.03.01-00-158/09-00]
- European Union within the European Regional Development Fund
Ethylbenzene dehydrogenase initiates the anaerobic bacterial degradation of ethylbenzene and propylbenzene. Although the enzyme is currently only known from a few closely related denitrifying bacterial strains affiliated to the Rhodocyclaceae, it clearly marks a universally occurring mechanism used for attacking recalcitrant substrates in the absence of oxygen. Ethylbenzene dehydrogenase belongs to subfamily 2 of the DMSO reductase-type molybdenum enzymes together with paralogous enzymes involved in the oxygen-independent hydroxylation of p-cymene, the isoprenoid side chains of sterols and even possibly n-alkanes; the subfamily also extends to dimethylsulfide dehydrogenases, selenite, chlorate and perchlorate reductases and, most significantly, dissimilatory nitrate reductases. The biochemical, spectroscopic and structural properties of the oxygen-independent hydroxylases among these enzymes are summarized and compared. All of them consist of three subunits, contain a molybdenum-bis-molybdopterin guanine dinucleotide cofactor, five Fe-S clusters and a heme b cofactor of unusual ligation, and are localized in the periplasmic space as soluble enzymes. In the case of ethylbenzene dehydrogenase, it has been determined that the heme b cofactor has a rather high redox potential, which may also be inferred for the paralogous hydroxylases. The known structure of ethylbenzene dehydrogenase allowed the calculation of detailed models of the reaction mechanism based on the density function theory as well as QM-MM (quantum mechanics-molecular mechanics) methods, which yield predictions of mechanistic properties such as kinetic isotope effects that appeared consistent with experimental data. (C) 2016 S. Karger AG, Basel
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