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

P Gouet; H M Jouve; P A Williams; I Andersson; P Andreoletti; L Nussaume; J Hajdu

doi:10.1038/nsb1196-951

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

Nat Struct Biol. 1996 Nov;3(11):951-6. doi: 10.1038/nsb1196-951.

Authors

P Gouet¹, H M Jouve, P A Williams, I Andersson, P Andreoletti, L Nussaume, J Hajdu

Affiliation

¹ Laboratory of Molecular Biophysics, University of Oxford, UK. [email protected]

PMID: 8901874
DOI: 10.1038/nsb1196-951

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Binding Sites
Catalase / chemistry*
Catalase / metabolism
Catalysis
Crystallography, X-Ray / methods*
Heme / metabolism
Iron / metabolism
Microspectrophotometry / methods*
Models, Molecular
NADP / metabolism
Proteus mirabilis / enzymology*

Substances

Heme
NADP
Iron
Catalase