Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy.
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.
Laboratory of Molecular Biophysics, University of Oxford, UK. patrice@biop.ox.ac.uk
P
P
Gouet
H M
HM
Jouve
P A
PA
Williams
I
I
Andersson
P
P
Andreoletti
L
L
Nussaume
J
J
Hajdu
D001665:Binding Sites; D002374:Catalase / Q000737:chemistry* / Q000378:metabolism; D002384:Catalysis; D018360:Crystallography, X-Ray / Q000379:methods*; D006418:Heme / Q000378:metabolism; D007501:Iron / Q000378:metabolism; D015591:Microspectrophotometry / Q000379:methods*; D008958:Models, Molecular; D009249:NADP / Q000378:metabolism; D011513:Proteus mirabilis / Q000201:enzymology*
D006418:Heme; D009249:NADP; D007501:Iron; D002374:Catalase