Probing the structure and bifunctionality of catalase-peroxidase (KatG)

Journal of Inorganic Biochemistry
Giulietta SmulevichChristian Obinger

Abstract

Catalase-peroxidases (KatGs) exhibit peroxidase and substantial catalase activities similar to monofunctional catalases. Crystal structures of four different KatGs reveal the presence of a peroxidase-conserved proximal and distal heme pocket together with features unique to KatG. To gain insight into their structure-function properties, many variants were produced and very similar results were obtained irrespective of the origin of the KatG mutated. This review focuses mainly on the electronic absorption and resonance Raman results together with the combined analysis of pre-steady and steady-state kinetics of various mutants involving both the peroxidase-conserved and the KatG-specific residues of recombinant KatG from the cyanobacterium Synechocystis. Marked differences in the structural role of conserved amino acids and hydrogen-bond networks in KatG with respect to the other plant peroxidases were found. Typically, the catalatic but not the peroxidatic activity was very sensitive to mutations that disrupted the KatG-typical extensive hydrogen-bonding network. Moreover, the integrity of this network is crucial for the formation of distinct protein radicals formed upon incubation of KatG with peroxides in the absence of one-el...Continue Reading

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Citations

Nov 17, 2007·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Tomomi Ten-ITakao Sato
May 24, 2008·Antioxidants & Redox Signaling·Marcel ZamockyChristian Obinger
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Jan 9, 2009·Journal of Experimental Botany·Margit BernroitnerChristian Obinger
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Apr 17, 2013·Archives of Microbiology·Marcel ZámockýBystrík Polek
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May 23, 2015·PLoS Neglected Tropical Diseases·Rahul TyagiMakedonka Mitreva
Jul 21, 2009·Biochemical Society Transactions·Marcel ZámockýChristian Obinger

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