@article{Reichenbecher1999Towar-7220,
  year={1999},
  doi={10.1016/S0167-4838(99)00004-7},
  title={Towards the reaction mechanism of pyrogallol-phloroglucinol transhydroxylase of Pelobacter acidigallici},
  number={2},
  volume={1430},
  issn={0167-4838},
  journal={Biochimica et Biophysica Acta / General subjects},
  pages={245--253},
  author={Reichenbecher, Wolfram and Schink, Bernhard}
}

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    <dc:contributor>Reichenbecher, Wolfram</dc:contributor>
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    <dc:creator>Schink, Bernhard</dc:creator>
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    <dcterms:title>Towards the reaction mechanism of pyrogallol-phloroglucinol transhydroxylase of Pelobacter acidigallici</dcterms:title>
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    <dcterms:bibliographicCitation>First publ. in: Biochimica et Biophysica Acta / General subjects, 1430 (1999), pp. 245-253</dcterms:bibliographicCitation>
    <dc:contributor>Schink, Bernhard</dc:contributor>
    <dcterms:abstract xml:lang="eng">Conversion of pyrogallol to phloroglucinol was studied with the molybdenum enzyme transhydroxylase of the strictly anaerobic fermenting bacterium Pelobacter acidigallici. Transhydroxylation experiments in H 2 18 O revealed that none of the hydroxyl groups of phloroglucinol was derived from water, confirming the concept that this enzyme transfers a hydroxyl group from the cosubstrate 1,2,3,5-tetrahydroxybenzene (tetrahydroxybenzene) to the acceptor pyrogallol, and simultaneously regenerates the cosubstrate. This concept requires a reaction which synthesizes the cofactor de novo to maintain a sufficiently high intracellular pool during growth. Some sulfoxides and aromatic N-oxides were found to act as hydroxyl donors to convert pyrogallol to tetrahydroxybenzene. Again, water was not the source of the added hydroxyl groups; the oxides reacted as cosubstrates in a transhydroxylation reaction rather than as true oxidants in a net hydroxylation reaction. No oxidizing agent was found that supported a formation of tetrahydroxybenzene via a net hydroxylation of pyrogallol. However, conversion of pyrogallol to phloroglucinol in the absence of tetrahydroxybenzene was achieved if little pyrogallol and a high amount of enzyme preparation was used which had been pre-exposed to air. Obviously, the enzyme was oxidized by air to form sufficient amounts of tetrahydroxybenzene from pyrogallol to start the reaction. A reaction mechanism is proposed which combines an oxidative hydroxylation with a reductive dehydroxylation via the molybdenum cofactor, and allows the transfer of a hydroxyl group between tetrahydroxybenzene and pyrogallol without involvement of water. With this, the transhydroxylase differs basically from all other hydroxylating molybdenum enzymes which all use water as hydroxyl source.</dcterms:abstract>
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