Nature Structural Biology
3, 951 - 956 (1996)
doi:10.1038/nsb1196-951
Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopyPatrice Gouet1, 6, Hélène-Marie Jouve2, Pamela A. Williams1, Inger Andersson3, Pierre Andreoletti2, Laurent Nussaume4
& Janos Hajdu1, 5, 7
1Laboratory of Molecular Biophysics and Oxford Centre for Molecular Sciences, University of Oxford, South Parks Road, Oxford OX1 3QU, UK
2Institut de Biologie Structural Jean-Pierre Ebel, Laboratoire d'Enzymologie Moléculaire(CNRS-CEA), 41 avenue des Martyrs, 38027 Grenoble Cedexl, France
3Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala Biomedical Center, P.O. Box 590, S-75124, Uppsala, Sweden
4Département d'Ecophysiologie végétale et de microbiologie. Centre d'Etudes Nucleates de Cadarache. 13108 Saint-Paul lez Durance Cedex, France
5Department of Biochemistry, Uppsala University, Box 576, S-751 23 Uppsala, Sweden
6patrice@biop.ox.ac.uk
7janos@biop.ox.ac.uk janos@xray.bmc.uu.se 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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