Literature DB >> 8901874

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

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

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.

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Year:  1996        PMID: 8901874     DOI: 10.1038/nsb1196-951

Source DB:  PubMed          Journal:  Nat Struct Biol        ISSN: 1072-8368


  12 in total

1.  Enzyme reactivation by hydrogen peroxide in heme-based tryptophan dioxygenase.

Authors:  Rong Fu; Rupal Gupta; Jiafeng Geng; Kednerlin Dornevil; Siming Wang; Yong Zhang; Michael P Hendrich; Aimin Liu
Journal:  J Biol Chem       Date:  2011-06-01       Impact factor: 5.157

2.  The structure of coral allene oxide synthase reveals a catalase adapted for metabolism of a fatty acid hydroperoxide.

Authors:  Michael L Oldham; Alan R Brash; Marcia E Newcomer
Journal:  Proc Natl Acad Sci U S A       Date:  2004-12-29       Impact factor: 11.205

3.  Resonance Raman spectroscopy of chloroperoxidase compound II provides direct evidence for the existence of an iron(IV)-hydroxide.

Authors:  Kari L Stone; Rachel K Behan; Michael T Green
Journal:  Proc Natl Acad Sci U S A       Date:  2006-08-08       Impact factor: 11.205

Review 4.  Human catalase: looking for complete identity.

Authors:  Madhur M Goyal; Anjan Basak
Journal:  Protein Cell       Date:  2010-11-09       Impact factor: 14.870

5.  Identification of a novel bond between a histidine and the essential tyrosine in catalase HPII of Escherichia coli.

Authors:  J Bravo; I Fita; J C Ferrer; W Ens; A Hillar; J Switala; P C Loewen
Journal:  Protein Sci       Date:  1997-05       Impact factor: 6.725

6.  The heat released during catalytic turnover enhances the diffusion of an enzyme.

Authors:  Clement Riedel; Ronen Gabizon; Christian A M Wilson; Kambiz Hamadani; Konstantinos Tsekouras; Susan Marqusee; Steve Pressé; Carlos Bustamante
Journal:  Nature       Date:  2014-12-10       Impact factor: 49.962

7.  The protonation status of compound II in myoglobin, studied by a combination of experimental data and quantum chemical calculations: quantum refinement.

Authors:  Kristina Nilsson; Hans-Petter Hersleth; Thomas H Rod; K Kristoffer Andersson; Ulf Ryde
Journal:  Biophys J       Date:  2004-08-31       Impact factor: 4.033

Review 8.  Cytochrome c oxidase as a proton-pumping peroxidase: reaction cycle and electrogenic mechanism.

Authors:  A A Konstantinov
Journal:  J Bioenerg Biomembr       Date:  1998-02       Impact factor: 2.945

Review 9.  Correlated single-crystal electronic absorption spectroscopy and X-ray crystallography at NSLS beamline X26-C.

Authors:  Allen M Orville; Richard Buono; Matt Cowan; Annie Héroux; Grace Shea-McCarthy; Dieter K Schneider; John M Skinner; Michael J Skinner; Deborah Stoner-Ma; Robert M Sweet
Journal:  J Synchrotron Radiat       Date:  2011-03-19       Impact factor: 2.616

10.  Spectroscopic description of an unusual protonated ferryl species in the catalase from Proteus mirabilis and density functional theory calculations on related models. Consequences for the ferryl protonation state in catalase, peroxidase and chloroperoxidase.

Authors:  O Horner; J-M Mouesca; P L Solari; M Orio; J-L Oddou; P Bonville; H M Jouve
Journal:  J Biol Inorg Chem       Date:  2007-01-20       Impact factor: 3.862

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