X-ray crystallography, mass spectrometry and single crystal microspectrophotometry: A multidisciplinary characterization of catechol 1,2 dioxygenase (original ) (raw )Fine-Tuning of Catalytic Properties of Catechol 1,2-Dioxygenase by Active Site Tailoring
Carlo Giunta , Raffaella Caglio , Enrica Pessione , Francesca Valetti
ChemBioChem, 2009
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Crystal structure of BphC, a halotolerant catechol dioxygenase
vipul solanki
2019
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X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. Implications for the extradiol cleavage mechanism
Lawrence Que
Biochemistry Usa, 1995
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Catechol 1,2-dioxygenase from the Gram-positive Rhodococcus opacus 1CP: Quantitative structure/activity relationship and the crystal structures of native enzyme and catechols adducts
Irene Matera
Journal of Structural Biology, 2010
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Spectroscopic studies of the catechol dioxygenases
Lawrence Que
Journal of Chemical Education, 1985
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A two-electron-shell game: intermediates of the extradiol-cleaving catechol dioxygenases
Lawrence Que
JBIC Journal of Biological Inorganic Chemistry, 2014
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Catalytic properties of catechol 1,2-dioxygenase from Acinetobacter radioresistens S13 immobilized on nanosponges
Gianfranco Gilardi
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Crystallization and preliminary crystallographic analysis of the catechol 2,3-dioxygenase PheB fromBacillus stearothermophilusBR219
Miki Senda
Acta crystallographica, 2006
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Crystal Structure of 4-Chlorocatechol 1,2-Dioxygenase from the Chlorophenol-utilizing Gram-positive Rhodococcus opacus 1CP
Marta Ferraroni
Journal of Biological Chemistry, 2004
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Substrate, substrate analogue, and inhibitor interactions with the ferrous active site of catechol 2,3-dioxygenase monitored through XAS studies
Andrea Scozzafava
FEBS Letters, 1994
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Structural roles of the active site iron(III) ions in catechol 1,2-dioxygenases and differential secondary structure changes in isoenzymes A and B from Acinetobacter radioresistens S13
Giovanna Nardo , Carlo Giunta , Enrica Pessione , Maria Cavaletto
Archives of Biochemistry and Biophysics, 2004
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Structure of catechol 1,2-dioxygenase from Pseudomonas arvilla
Lawrence Que
Biochemical and Biophysical Research Communications, 2005
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The Role of the Conserved Residues His-246, His-199, and Tyr-255 in the Catalysis of Catechol 2,3-Dioxygenase from Pseudomonas stutzeri OX1
Leila Birolo
Journal of Biological Chemistry, 2004
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Purification, biochemical properties and substrate specificity of a catechol 1,2-dioxygenase from a phenol degrading Acinetobacter radioresistens
Carlo Giunta , Enrica Pessione
FEBS Letters, 1997
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EPR Studies of Chlorocatechol 1,2-Dioxygenase: Evidences of Iron Reduction during Catalysis and of the Binding of Amphipatic Molecules
Andressa Pinto , Ana Araujo
Biophysical Journal, 2005
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Purification and catalytic properties of two catechol 1,2-dioxygenase isozymes from benzoate-grown cells of Acinetobacter radioresistens
Carlo Giunta , Enrica Pessione
Journal of protein chemistry, 2000
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Crystal Structure of 3-Chlorocatechol 1,2-dioxygenase Key Enzyme of a New Modified Ortho-pathway from the Gram-positive Rhodococcus opacus 1CP Grown on 2-chlorophenol
Andrea Scozzafava
Journal of Molecular Biology, 2006
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Homology modeling and docking studies of Catechol-2,3-dioxygenase
Abdullahi T Ajao , Dr. Kannan M
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Structures of an extradiol catechol dioxygenase – C23O64, from 3-nitrotoluene degrading Diaphorobacter sp. strain DS2 in substrate-free, substrate-bound and substrate analog-bound states
gurunath ramanathan
Experimental Results
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Iron(III)−Catecholato Complexes as Structural and Functional Models of the Intradiol-Cleaving Catechol Dioxygenases
Gerard Van Koten , Robertus Klein Gebbink
Inorganic Chemistry, 2007
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A Novel [2Fe-2S] Ferredoxin from Pseudomonas putida mt2 Promotes the Reductive Reactivation of Catechol 2,3-Dioxygenase
Jacques Gaillard
Journal of Biological Chemistry, 1998
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A hyperactive cobalt-substituted extradiol-cleaving catechol dioxygenase
Lawrence Que
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2011
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Iron(III) Complexes of Sterically Hindered Tetradentate Monophenolate Ligands as Functional Models for Catechol 1,2-Dioxygenases: The Role of Ligand Stereoelectronic Properties
Marappan Velusamy
Inorganic Chemistry, 2004
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In vivo reactivation of catechol 2,3-dioxygenase mediated by a chloroplast-type ferredoxin: a bacterial strategy to expand the substrate specificity of aromatic degradative pathways
Alessandra Polissi
The EMBO Journal, 1993
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Spectroscopic Studies of the Anaerobic Enzyme−Substrate Complex of Catechol 1,2-Dioxygenase
Thomas Spiro
Journal of the American Chemical Society, 2005
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