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Acetylene Hydratase : Part 5. Molybdenum/Tungsten

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2008

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Seiffert, Grazyna B.
Abt, Dietmar
Fischer, David
Einsle, Oliver

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https://doi.org/10.1002/0470028637.met231
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MESSERSCHMIDT, Albrecht, ed.. Handbook of Metalloproteins. Chichester, UK: John Wiley & Sons, Ltd, 2008. ISBN 978-0-470-86981-9. Available under: doi: 10.1002/0470028637.met231

Zusammenfassung

The tungsten-iron-sulfur enzyme acetylene hydratase is a rather unique enzyme within the class of tungsten/molybdenum enzymes in the sense that it catalyzes a nonredox reaction, the addition of one molecule of water to the C[TRIPLE BOND]C bond of acetylene to form acetaldehyde. Its crystal structure (1.26 Å) reveals a close to octahedral, or trigonal antiprismatic tungsten center, which binds a water molecule that gets activated by an adjacent aspartate residue such that it can attack an acetylene molecule bound in a distinct, hydrophobic pocket. This requires a strong shift of pKa of the aspartate, caused by a nearby low-potential [4Fe–4S] cluster. To gain access to this novel W-Asp-active site, the protein evolved a new substrate channel distant from where it is found in other molybdenum and tungsten enzymes.

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570 Biowissenschaften, Biologie

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ISO 690SEIFFERT, Grazyna B., Dietmar ABT, Felix TENBRINK, David FISCHER, Oliver EINSLE, Peter M. H. KRONECK, 2008. Acetylene Hydratase : Part 5. Molybdenum/Tungsten. In: MESSERSCHMIDT, Albrecht, ed.. Handbook of Metalloproteins. Chichester, UK: John Wiley & Sons, Ltd, 2008. ISBN 978-0-470-86981-9. Available under: doi: 10.1002/0470028637.met231
BibTex
@incollection{Seiffert2008Acety-39244,
  year={2008},
  doi={10.1002/0470028637.met231},
  title={Acetylene Hydratase : Part 5. Molybdenum/Tungsten},
  isbn={978-0-470-86981-9},
  publisher={John Wiley & Sons, Ltd},
  address={Chichester, UK},
  booktitle={Handbook of Metalloproteins},
  editor={Messerschmidt, Albrecht},
  author={Seiffert, Grazyna B. and Abt, Dietmar and tenBrink, Felix and Fischer, David and Einsle, Oliver and Kroneck, Peter M. H.}
}
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    <dcterms:abstract xml:lang="eng">The tungsten-iron-sulfur enzyme acetylene hydratase is a rather unique enzyme within the class of tungsten/molybdenum enzymes in the sense that it catalyzes a nonredox reaction, the addition of one molecule of water to the C[TRIPLE BOND]C bond of acetylene to form acetaldehyde. Its crystal structure (1.26 Å) reveals a close to octahedral, or trigonal antiprismatic tungsten center, which binds a water molecule that gets activated by an adjacent aspartate residue such that it can attack an acetylene molecule bound in a distinct, hydrophobic pocket. This requires a strong shift of pKa of the aspartate, caused by a nearby low-potential [4Fe–4S] cluster. To gain access to this novel W-Asp-active site, the protein evolved a new substrate channel distant from where it is found in other molybdenum and tungsten enzymes.</dcterms:abstract>
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