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Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy

Nature Structural Biologyvolume 3pages951956 (1996) | Download Citation

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Abstract

Various enzymes use semi-stable ferryl intermediates and free radicals during their catalytic cycle, amongst them haem catalases. Structures for two transient intermediates (compounds I and II) of the NADPH-dependent catalase from Proteus mirabilis (PMC) have been determined by time-resolved X-ray crystallography and single crystal microspectrophotometry. The results show the formation and transformation of the ferryl group in the haem, and the unexpected binding of an anion during this reaction at a site distant from the haem.

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Author information

Affiliations

  1. Laboratory of Molecular Biophysics and Oxford Centre for Molecular Sciences, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK

    • Patrice Gouet
    • , Pamela A. Williams
    •  & Janos Hajdu
  2. Institut de Biologie Structural Jean-Pierre Ebel, Laboratoire d'Enzymologie Moléculaire(CNRS-CEA), 41 avenue des Martyrs, 38027, Grenoble Cedexl, France

    • Hélène-Marie Jouve
    •  & Pierre Andreoletti
  3. Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala Biomedical Center, P.O. Box 590, S-75124, Uppsala, Sweden

    • Inger Andersson
  4. Département d'Ecophysiologie végétale et de microbiologie, Centre d'Etudes Nucleates de Cadarache, 13108, Saint-Paul lez Durance Cedex, France

    • Laurent Nussaume
  5. Department of Biochemistry, Uppsala University, Box 576, S-751 23, Uppsala, Sweden

    • Janos Hajdu

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https://doi.org/10.1038/nsb1196-951

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