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    Nat Struct Biol. 1996 Nov;3(11):951-6.

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

    Gouet P, Jouve HM, Williams PA, Andersson I, Andreoletti P, Nussaume L, Hajdu J.

    Laboratory of Molecular Biophysics, University of Oxford, UK. patrice@biop.ox.ac.uk

    Comment in:

    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.

    PMID: 8901874 [PubMed - indexed for MEDLINE]

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