Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy
- 1 November 1996
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 3 (11) , 951-956
- https://doi.org/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.Keywords
This publication has 33 references indexed in Scilit:
- Laue Crystallography: It's show timeCurrent Biology, 1995
- Crystal Structure ofProteus mirabilisPR Catalase With and Without Bound NADPHJournal of Molecular Biology, 1995
- Crystal structure of catalase HPII from Escherichia coliStructure, 1995
- Complete amino acid sequence ofProteus mirabilis PR catalase. Occurrence of a methionine sulfone in the close proximity of the active siteProtein Journal, 1995
- Reactions of Bovine Liver Catalase with Superoxide Radicals and Hydrogen PeroxideFree Radical Research, 1995
- A fast and portable microspectrophotometer for protein crystallographyJournal of Applied Crystallography, 1993
- A mechanism for NADPH inhibition of catalase compound II formationFEBS Letters, 1992
- Three‐dimensional structure of catalase from Micrococcus lysodeikticus at 1.5 Å resolutionFEBS Letters, 1992
- The refined structure of beef liver catalase at 2·5 Å resolutionActa crystallographica Section B, Structural science, crystal engineering and materials, 1986
- Cytochrome c peroxidase compound ES is identical with horseradish peroxidase compound I in iron-ligand distancesBiochemistry, 1986