page_title: Ethylbenzene hydroxylase
section_title: Structural studies
hierarchical_section_title: Ethylbenzene hydroxylase / Structural studies
caption_attribution_description: English: The crystal structure of ethylbenzene dehydrogenase from Aromatoleum aromaticum (EbN1). Green - alpha subunit, blue - beta subunit, red - gamma subunit
context_page_description: In enzymology, an ethylbenzene hydroxylase is an enzyme that catalyzes the chemical reaction
  ethylbenzene + H₂O + acceptor -1-phenylethanol + reduced acceptor
  The 3 substrates of this enzyme are ethylbenzene, H₂O, and acceptor, whereas its two products are-1-phenylethanol and reduced acceptor.
  This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH₂ groups with other acceptors. The systematic name of this enzyme class is ethylbenzene:acceptor oxidoreductase. Other names in common use include ethylbenzene dehydrogenase, and ethylbenzene: oxidoreductase. This enzyme participates in ethylbenzene degradation by Aromatoleum aromaticum, a denitrifying bacterium related to the genera Azoarcus and Thauera. It is a molybdenum enzyme belonging to the DMSO reductase family. Molybdenum enzymes are distinguished by the presence of a unique active site containing molybdenum atom, one or two molybdopterins and additional ligands. EBDH is synthesized exclusively in cells grown anaerobically on ethylbenzene and has been identified as a soluble periplasmic protein.
context_section_description: As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2IVF. EBDH consists of three subunits of 96, 43, and 23 kDa, and contains a molybdenum cofactor and a heme b559 cofactor linked by a linear row of five iron-sulfur clusters.
caption: Structure of ethylbenzene dehydrogenase
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