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Evolution of catalases from bacteria to humans.
An overview of the distribution, phylogeny, structure, and function of heme enzymes is presented, including typical catalases and catalase-peroxidases, which are found in plants and animals and exhibit both catalatic and peroxidatic activities.
Active site structure and catalytic mechanisms of human peroxidases.
Myeloperoxidase: a target for new drug development?
- E. Malle, P. Furtmüller, W. Sattler, C. Obinger
- Biology, ChemistryBritish journal of pharmacology
- 1 November 2007
Detailed information on the structure of ferric MPO and its complexes with low‐ and high‐spin ligands is available enables a rationale attempt in developing specific MPO inhibitors that still maintain MPO activity during host defence and bacterial killing but interfere with pathophysiologically persistent activation of MPO.
Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate.
The results show that thiocyanate is an important substrate of myeloperoxidase in most environments and that hypothiocianate is likely to contribute to leukocyte antimicrobial activity.
Occurrence, phylogeny, structure, and function of catalases and peroxidases in cyanobacteria.
- M. Bernroitner, M. Zámocký, P. Furtmüller, G. Peschek, C. Obinger
- BiologyJournal of experimental botany
- 1 February 2009
It is demonstrated that H(2)O(2)-dismutating enzymes are mainly represented by bifunctional (haem) catalase-peroxidases and (binuclear) manganese catalases, with the latter being almost exclusively found in diazotrophic species.
Activity, peroxide compound formation, and heme d synthesis in Escherichia coli HPII catalase.
- C. Obinger, M. Maj, P. Nicholls, P. Loewen
- Chemistry, BiologyArchives of biochemistry and biophysics
- 1 June 1997
HPII Asn201, like the corresponding residue in protoheme catalases, may promote H+ transfer to His128 imidazole, facilitating peroxide anion binding to heme and stabilization of a transition state for heterolytic cleavage of the O-O bond.
The peroxidase–cyclooxygenase superfamily: Reconstructed evolution of critical enzymes of the innate immune system
The presented data unequivocally suggest that predecessor genes of mammalian heme peroxidases have segregated very early in evolution, showing that even in certain prokaryotic organisms, genes encoding putative antimicrobial enzymes are found providing a group of bacteria with an evolutionary advantage over the others.
Purification and Characterization of a Homodimeric Catalase-Peroxidase from the CyanobacteriumAnacystis nidulans☆☆☆
Cytosolic extracts of the cyanobacterium Anacystis nidulansexhibit both catalase and o-dianisidine peroxidase activity, and demonstrates one distinct enzyme, which has been purified to essential homogeneity and found to be composed of two identical subunits of equal size.
Reaction of lactoperoxidase compound I with halides and thiocyanate.
- P. Furtmüller, W. Jantschko, G. Regelsberger, C. Jakopitsch, J. Arnhold, C. Obinger
- 20 August 2002
This study for the first time presents transient kinetic measurements of the reactivity of its competent redox intermediate compound I with halides and thiocyanate, using the sequential stopped-flow technique.
The Iron Superoxide Dismutase from the Filamentous Cyanobacterium Nostoc PCC 7120
A phylogenetic analysis of FeSODs shows that cyanobacterial enzymes form a well separated cluster with filamentous species found in one subcluster and unicellular species in the other, and that FeS OD is localized in the cytosol of vegetative cells and heterocysts (nitrogenase containing specialized cells formed during nitrogen-limiting conditions).