Role of the Main Access Channel of Catalase-Peroxidase in Catalysis*

No abstract is available for this paper.

• Publication year

  2005

• Venue

  Journal of Biological Chemistry

• Publication date

  2005-12-23

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1074/jbc.M508009200PMID 16244360
• 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.

• Kinetics of Interconversion of Ferrous Enzymes, Compound II and Compound III, of Wild-type Synechocystis Catalase-peroxidase and Y249F

  2005cited by this paper
• Correlation between isoniazid resistance and superoxide reactivity in mycobacterium tuberculosis KatG.

  2005cited by this paper
• Fifteen years of Raman spectroscopy of engineered heme containing peroxidases: what have we learned?

  2005cited by this paper
• Comparison between catalase-peroxidase and cytochrome c peroxidase. The role of the hydrogen-bond networks for protein stability and catalysis.

  2004cited by this paper
• Influence of the Unusual Covalent Adduct on the Kinetics and Formation of Radical Intermediates in Synechocystis Catalase Peroxidase

  2004cited by this paper
• Catalase Reaction by Myoglobin Mutants and Native Catalase

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

  2004cited by this paper
• Purification and characterization of Mycobacterium tuberculosis KatG, KatG(S315T), and Mycobacterium bovis KatG(R463L).

  2004cited by this paper
• Relationship between heme vinyl conformation and the protein matrix in peroxidases

  2003cited by this paper
• Protein-based radicals in the catalase-peroxidase of synechocystis PCC6803: a multifrequency EPR investigation of wild-type and variants on the environment of the heme active site.

  2003cited by this paper
• Distal site aspartate is essential in the catalase activity of catalase-peroxidases.

  2003cited by this paper
• Catalase-peroxidase KatG of Burkholderia pseudomallei at 1.7A resolution.

  2003cited by this paper
• Total Conversion of Bifunctional Catalase-Peroxidase (KatG) to Monofunctional Peroxidase by Exchange of a Conserved Distal Side Tyrosine*

  2003cited by this paper
• An Electrical Potential in the Access Channel of Catalases Enhances Catalysis*

  2003cited by this paper
• Reduced Affinity for Isoniazid in the S315T Mutant ofMycobacterium tuberculosis KatG Is a Key Factor in Antibiotic Resistance*

  2003cited by this paper
• Engineering the proximal heme cavity of catalase-peroxidase.

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

  2002cited by this paper
• New insights into the heme cavity structure of catalase-peroxidase: a spectroscopic approach to the recombinant synechocystis enzyme and selected distal cavity mutants.

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

  2002cited by this paper
• The role of distal tryptophan in the bifunctional activity of catalase-peroxidases.

  2001cited by this paper
• Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism.

  2000cited by this paper
• Effect of Distal Cavity Mutations on the Formation of Compound I in Catalase-Peroxidases*

  2000cited by this paper
• Mutants That Alter the Covalent Structure of Catalase Hydroperoxidase II from Escherichia coli*

  1999cited by this paper
• Structure of catalase-A from Saccharomyces cerevisiae.

  1999cited by this paper
• Catalase-Peroxidase from the Cyanobacterium Synechocystis PCC 6803: Cloning, Overexpression in Escherichia coli, and Kinetic Characterization

  1999cited by this paper
• Assignment of Protoheme Resonance Raman Spectrum by Heme Labeling in Myoglobin

  1996cited by this paper
• Superfamily of plant, fungal and bacterial peroxidases

  1992cited by this paper
• Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily.

  1991cited by this paper
• Calculation of protein extinction coefficients from amino acid sequence data.

  1989cited by this paper

• Detecting rotational disorder in heme proteins: A comparison between resonance Raman spectroscopy, nuclear magnetic resonance, and circular dichroism

  2021cites this paper
• Protein‐Derived Cofactors

  2020cites this paper
• Catalase and its mysteries.

  2018cites this paper
• Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.

  2018cites this paper
• Biophysical insights into dietary antioxidants as cyclooxygenase modulators

  2018cites this paper
• Insights on the Mechanism of Action of INH-C10 as an Antitubercular Prodrug.

  2017cites this paper
• The Catalase Activity of Catalase-Peroxidases Is Modulated by Changes in the pKa of the Distal Histidine.

  2017cites this paper
• Mutual synergy between catalase and peroxidase activities of the bifunctional enzyme KatG is facilitated by electron hole-hopping within the enzyme

  2017cites this paper
• Ultraviolet–Visible (UV-Vis) and Fluorescence Spectroscopic Investigation of the Interactions of Ionic Liquids and Catalase

  2016cites this paper
• Comparative study of enzymatic activities of new KatG mutants from low- and high-level isoniazid-resistant clinical isolates of Mycobacterium tuberculosis.

  2016cites this paper
• Resolving the Paradoxical Nature of a Bifunctional Enzyme: Pathways and Regulation of Intramolecular Electron Transfer In KatG

  2016cites this paper
• A role for catalase-peroxidase large loop 2 revealed by deletion mutagenesis: control of active site water and ferric enzyme reactivity.

  2015cites this paper
• Catalase in peroxidase clothing: Interdependent cooperation of two cofactors in the catalytic versatility of KatG.

  2014cites this paper
• KATG as a Defense Against Hydrogen Peroxide Toxicity: From a Redundant C-Terminal Domain to the Paradoxical Synergy of Two Mututally Antagonistic Activities

  2014cites this paper
• Computational study on ruthenium anticancer complexes in the presence of Reactive Oxygen Species

  2013cites this paper
• High‐throughput molecular dynamics simulations: toward a dynamic view of macromolecular structure

  2013cites this paper
• Synergy not Antagonism in Antioxidant Defenses: The Unanticipated Effect of Electron Donors on Catalase-peroxidase Function

  2013cites this paper
• Enhancing the peroxidatic activity of KatG by deletion mutagenesis.

  2012cites this paper
• Gene Duplication and Fusion: Strategy for Active Site Control and Starting Point for New Catalysts

  2012cites this paper
• Roles of Large Loops in Catalytic Versatility of Catalase-Peroxidases: Significance of Peripheral Structures in Improvising Enzyme Functions

  2012influential citation
• Hydrogen Peroxide Degradation in Cyanobacteria

  2011cites this paper
• Probing hydrogen peroxide oxidation kinetics of wild-type Synechocystis catalase-peroxidase (KatG) and selected variants.

  2010cites this paper
• Mechanisms of catalase activity of heme peroxidases.

  2010cites this paper
• Disruption of the H-bond network in the main access channel of catalase-peroxidase modulates enthalpy and entropy of Fe(III) reduction.

  2010cites this paper
• Pathways and mechanisms for product release in the engineered haloalkane dehalogenases explored using classical and random acceleration molecular dynamics simulations.

  2009cites this paper
• Role of the Oxyferrous Heme Intermediate and Distal Side Adduct Radical in the Catalase Activity of Mycobacterium tuberculosis KatG Revealed by the W107F Mutant*

  2009cites this paper
• The Reaction of Synechocystis Catalase–Peroxidase (KatG) with Isoniazid Investigated by Multifrequency (9–285 GHz) EPR Spectroscopy

  2009cites this paper
• Toward the understanding of complex biochemical systems: The significance of global protein structure and thorough parametric analysis

  2009cites this paper
• An Oxyferrous Heme/Protein-based Radical Intermediate Is Catalytically Competent in the Catalase Reaction of Mycobacterium tuberculosis Catalase-Peroxidase (KatG)*

  2009cites this paper
• Occurrence, phylogeny, structure, and function of catalases and peroxidases in cyanobacteria.

  2009cites this paper
• Comparative study of catalase-peroxidases (KatGs).

  2008cites this paper
• Impact of distal side water and residue 315 on ligand binding to ferric Mycobacterium tuberculosis catalase-peroxidase (KatG).

  2008cites this paper
• Toward efficient nanoporous catalysts: controlling site-isolation and concentration of grafted catalytic sites on nanoporous materials with solvents and colorimetric elucidation of their site-isolation.

  2008cites this paper
• MolAxis: a server for identification of channels in macromolecules

  2008cites this paper
• The One-electron Autoxidation of Human Cytochrome P450 3A4*

  2007cites this paper
• Redox intermediates in the catalase cycle of catalase-peroxidases from Synechocystis PCC 6803, Burkholderia pseudomallei, and Mycobacterium tuberculosis.

  2007cites this paper
• Hydrogen peroxide oxidation by catalase‐peroxidase follows a non‐scrambling mechanism

  2007cites this paper
• Radical Sites in Mycobacterium tuberculosis KatG Identified Using Electron Paramagnetic Resonance Spectroscopy, the Three-dimensional Crystal Structure, and Electron Transfer Couplings*

  2007cites this paper
• Probing the structure and bifunctionality of catalase-peroxidase (KatG).

  2006cites this paper
• Redox thermodynamics of the ferric-ferrous couple of wild-type synechocystis KatG and KatG(Y249F).

  2006cites this paper
• Two alternative substrate paths for compound I formation and reduction in catalase–peroxidase KatG from Burkholderia pseudomallei

  2006influential citation
• Advances and Applications in Bioinformatics and Chemistry Dovepress Molecular Dynamics Simulations: Advances and Applications

  year unknowncites this paper