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Publication Detail
Aerobic damage to [FeFe]-hydrogenases: Activation barriers for the chemical attachment of O2
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Kubas A, De Sancho D, Best RB, Blumberger J
  • Publication date:
  • Pagination:
    4081, 4084
  • Journal:
    Angewandte Chemie - International Edition
  • Volume:
  • Issue:
  • Status:
  • Print ISSN:
[FeFe]-hydrogenases are the best natural hydrogen-producing enzymes but their biotechnological exploitation is hampered by their extreme oxygen sensitivity. The free energy profile for the chemical attachment of O to the enzyme active site was investigated by using a range-separated density functional re-parametrized to reproduce high-level ab initio data. An activation free-energy barrier of 13 kcal mol was obtained for chemical bond formation between the di-iron active site and O , a value in good agreement with experimental inactivation rates. The oxygen binding can be viewed as an inner-sphere electron-transfer process that is strongly influenced by Coulombic interactions with the proximal cubane cluster and the protein environment. The implications of these results for future mutation studies with the aim of increasing the oxygen tolerance of this enzyme are discussed. Clearing the air: The free energy profiles for the chemical attachment of O to the active sites of [FeFe]-hydrogenases from Clostridium pasteurianum and Desulfovibrio desulfuricans were investigated. Based on the results, possible target sites for future mutation studies were suggested that may reduce oxygen binding and thus the oxygen sensitivity of these enzymes. © 2014 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. 2 2 2 -1
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