Probing the two-domain structure of homodimeric prokaryotic and eukaryotic catalase-peroxidases.

No abstract is available for this paper.

• Publication year

  2010

• Venue

  Biochimica et Biophysica Acta

• Publication date

  2010-11-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/j.bbapap.2010.07.013PMID 20654740PMCID PMC3513708
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Molecular Phylogeny of Heme Peroxidases

  2010cited by this paper
• Mechanisms of catalase activity of heme peroxidases.

  2010cited by this paper
• Euglena gracilis ascorbate peroxidase forms an intramolecular dimeric structure: its unique molecular characterization.

  2010cited by this paper
• Evolution of structure and function of Class I peroxidases.

  2010cited by this paper
• Biocatalysis based on heme peroxidases : peroxidases as potential industrial biocatalysts

  2010cited by this paper
• Two distinct groups of fungal catalase/peroxidases.

  2009cited by this paper
• Intracellular catalase/peroxidase from the phytopathogenic rice blast fungus Magnaporthe grisea: expression analysis and biochemical characterization of the recombinant protein.

  2009cited by this paper
• Prokaryotic origins of the non-animal peroxidase superfamily and organelle-mediated transmission to eukaryotes.

  2007cited by this paper
• Phylogenetic distribution of catalase-peroxidases: are there patches of order in chaos?

  2007cited by this paper
• Catalase-peroxidase active site restructuring by a distant and "inactive" domain.

  2006cited by this paper
• Probing the structure and bifunctionality of catalase-peroxidase (KatG).

  2006cited by this paper
• Phylogenetic relationships in class I of the superfamily of bacterial, fungal, and plant peroxidases.

  2004cited by this paper
• Properties of catalase-peroxidase lacking its C-terminal domain.

  2004cited by this paper
• Structure of the C-terminal domain of the catalase-peroxidase KatG from Escherichia coli.

  2004cited by this paper
• Crystal Structure of Mycobacterium tuberculosis Catalase-Peroxidase*

  2004cited by this paper
• Catalase-peroxidase KatG of Burkholderia pseudomallei at 1.7A resolution.

  2003cited by this paper
• The molecular evolution of catalatic hydroperoxidases: evidence for multiple lateral transfer of genes between prokaryota and from bacteria into eukaryota.

  2003cited by this paper
• Crystallization and preliminary X-ray analysis of the hydroperoxidase I C-terminal domain from Escherichia coli.

  2002cited by this paper
• The 2.0 Å crystal structure of catalase-peroxidase from Haloarcula marismortui

  2002cited by this paper
• Thermal Unfolding of Soybean Peroxidase

  2002cited by this paper
• Crystallization and preliminary X-ray diffraction studies of catalase-peroxidase from Synechococcus PCC 7942.

  2002cited by this paper
• The molecular peculiarities of catalase‐peroxidases

  2001cited by this paper
• Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles.

  2000cited by this paper
• Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles.

  2000cited by this paper
• Catalase-Peroxidase from the Cyanobacterium Synechocystis PCC 6803: Cloning, Overexpression in Escherichia coli, and Kinetic Characterization

  1999cited by this paper
• Conformational states in denaturants of cytochrome c and horseradish peroxidases examined by fluorescence and circular dichroism.

  1998influential reference
• The role of quaternary interactions on the stability and activity of ascorbate peroxidase

  1998cited by this paper
• Site‐directed mutagenesis of the lower parts of the major substrate channel of yeast catalase A leads to highly increased peroxidatic activity

  1995cited by this paper
• Thermodynamics of denaturation of barstar: evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride.

  1995cited by this paper
• Stationary and time-resolved circular dichroism of hemoglobins.

  1994cited by this paper
• Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition.

  1991cited by this paper
• Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily.

  1991cited by this paper
• Fluorescence decay kinetics of the tryptophyl residues of myoglobin: effect of heme ligation and evidence for discrete lifetime components.

  1990cited by this paper
• Calorimetric studies of the thermal denaturation of cytochrome c peroxidase.

  1988cited by this paper
• FLUORESCENCE AND THE LOCATION OF TRYPTOPHAN RESIDUES IN PROTEIN MOLECULES

  1973cited by this paper
• The origin of the heme Cotton effects in myoglobin and hemoglobin.

  1971cited by this paper
• The origin of the heme Cotton effects in myoglobin and hemoglobin.

  1971cited by this paper
• A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase.

  1952cited by this paper

• Deciphering Isoniazid Drug Resistance Mechanisms on Dimeric Mycobacterium tuberculosis KatG via Post-molecular Dynamics Analyses Including Combined Dynamic Residue Network Metrics

  2022cites this paper
• A bifunctional catalase‐peroxidase, MakatG1, contributes to virulence of Metarhizium acridum by overcoming oxidative stress on the host insect cuticle

  2017cites this paper
• Interaction with the Redox Cofactor MYW and Functional Role of a Mobile Arginine in Eukaryotic Catalase-Peroxidase

  2016cites this paper
• Integral role of the I'-helix in the function of the "inactive" C-terminal domain of catalase-peroxidase (KatG).

  2013cites this paper
• High Conformational Stability of Secreted Eukaryotic Catalase-peroxidases

  2012influential citation
• Gene Duplication and Fusion: Strategy for Active Site Control and Starting Point for New Catalysts

  2012influential citation
• Eukaryotic extracellular catalase–peroxidase from Magnaporthe grisea – Biophysical/chemical characterization of the first representative from a novel phytopathogenic KatG group

  2012cites this paper