ArticleBiochimie2012
Eukaryotic extracellular catalase-peroxidase from Magnaporthe grisea - Biophysical/chemical characterization of the first representative from a novel phytopathogenic KatG group.
Article in Biochimie, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Antioxidant Systems of Plant Pathogenic Fungi: Functions in Oxidative Stress Response and Their Regulatory Mechanisms.The plant pathology journal · 2024Review
- Unraveling the evolutionary origin of theFrontiers in molecular biosciences · 2024Article
- Tetracarboxylic acid transporter regulates growth, conidiation, and carbon utilization in Metarhizium acridum.Applied microbiology and biotechnology · 2023Article
- Monofunctional Heme-Catalases.Antioxidants (Basel, Switzerland) · 2022Review
- Hybrid Heme Peroxidases from Rice Blast FungusAntioxidants (Basel, Switzerland) · 2020Article
- Genome sequence of the filamentous soil fungus Chaetomium cochliodes reveals abundance of genes for heme enzymes from all peroxidase and catalase superfamilies.BMC genomics · 2016Article
- Interaction with the Redox Cofactor MYW and Functional Role of a Mobile Arginine in Eukaryotic Catalase-Peroxidase.Biochemistry · 2016Article
- Independent evolution of four heme peroxidase superfamilies.Archives of biochemistry and biophysics · 2015Article
- Article
- Redundant catalases detoxify phagocyte reactive oxygen and facilitate Histoplasma capsulatum pathogenesis.Infection and immunity · 2013Article
- Intracellular targeting of ascomycetous catalase-peroxidases (KatG1s).Archives of microbiology · 2013Article
- Molecular evolution of hydrogen peroxide degrading enzymes.Archives of biochemistry and biophysics · 2012Review
- High conformational stability of secreted eukaryotic catalase-peroxidases: answers from first crystal structure and unfolding studies.The Journal of biological chemistry · 2012Article
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Authors and funding
9 authors.
Funding
Abstract
All phytopathogenic fungi have two catalase-peroxidase paralogues located either intracellularly (KatG1) or extracellularly (KatG2). Here, for the first time a secreted bifunctional, homodimeric catalase-peroxidase (KatG2 from the rice blast fungus Magnaporthe grisea) has been produced heterologously with almost 100% heme occupancy and comprehensively investigated by using a broad set of methods including UV-Vis, ECD and resonance Raman spectroscopy (RR), thin-layer spectroelectrochemistry, mass spectrometry, steady-state & presteady-state spectroscopy. RR spectroscopy reveals that MagKatG2 shows a unique mixed-spin state, non-planar heme b, and a proximal histidine with pronounced imidazolate character. At pH 7.0 and 25 °C, the standard reduction potential E°' of the Fe(III)/Fe(II) couple for the high-spin native protein was found to fall in the range typical for the KatG family. Binding of cyanide was relatively slow at pH 7.0 and 25 °C and with a K(d) value significantly higher than for the intracellular counterpart. Demonstrated by mass spectrometry MagKatG2 has the typical Trp118-Tyr251-Met277 adduct that is essential for its predominantly catalase activity at the unique acidic pH optimum. In addition, MagKatG2 acts as a versatile peroxidase using both one- and two-electron donors. Based on these data, structure-function relationships of extracellular eukaryotic KatGs are discussed with respect to intracellular KatGs and possible role(s) in host-pathogen interaction.
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