Kinetic and spectroscopic studies of cobalt- and manganese-substituted extradiol-cleaving homoprotocatechuate 2,3-dioxygenases
Jay Fielding
2013
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Characterization of an O2 adduct of an active cobalt-substituted extradiol-cleaving catechol dioxygenase
Lawrence Que
Journal of the American Chemical Society, 2012
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Swapping metals in Fe- and Mn-dependent dioxygenases: Evidence for oxygen activation without a change in metal redox state
Lawrence Que
Proceedings of the National Academy of Sciences, 2008
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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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X-ray crystallography, mass spectrometry and single crystal microspectrophotometry: A multidisciplinary characterization of catechol 1,2 dioxygenase
Barbara Pioselli, Stefano Bruno
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2011
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Nickel replacing iron in the metal binding site of catechol 2, 3 dioxygenase (C23O) found to enhance enzyme activity
IJOAR Journal
A. Jayashree and A. Murugan
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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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Synthetic models for catechol 1,2-dioxygenases. Interception of a metal catecholate-dioxygen adduct
Carlo Mealli
Journal of the American Chemical Society, 1991
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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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Spectroscopic studies of the catechol dioxygenases
Lawrence Que
Journal of Chemical Education, 1985
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Intersubunit interaction and catalytic activity of catechol 2,3-dioxygenases
Shigeaki Harayama
Biochemical Journal, 2003
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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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Oxy Intermediates of Homoprotocatechuate 2,3-Dioxygenase: Facile Electron Transfer between Substrates
Joseph Dalluge
Biochemistry, 2011
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Homology modeling and docking studies of Catechol-2,3-dioxygenase
Abdullahi T Ajao, Dr. Kannan M
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Substrate-Assisted O2 Activation in a Cofactor-Independent Dioxygenase
Reinhard Kappl
Chemistry & Biology, 2014
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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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In vivo self-hydroxylation of an iron-substituted manganese-dependent extradiol cleaving catechol dioxygenase
Lawrence Que
JBIC Journal of Biological Inorganic Chemistry, 2011
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Modeling the 2-His-1-Carboxylate Facial Triad: Iron−Catecholato Complexes as Structural and Functional Models of the Extradiol Cleaving Dioxygenases
Gerard Van Koten, Robertus Klein Gebbink
Journal of the American Chemical Society, 2007
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Insights into the binding interaction of substrate with catechol 2,3-dioxygenase from biophysics point of view
Ming Wong
Journal of Hazardous Materials, 2020
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Iron(III) Complexes of Tripodal Monophenolate Ligands as Models for Non-Heme Catechol Dioxygenase Enzymes: Correlation of Dioxygenase Activity with Ligand Stereoelectronic Properties
Suresh Eringathodi
Inorganic Chemistry, 2009
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Crystal structure of BphC, a halotolerant catechol dioxygenase
vipul solanki
2019
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Catalytic activation of dioxygen by oximatocobalt(II) and oximatoiron(II) complexes for catecholase-mimetic oxidations of o-substituted phenols
Zoltán May
Coordination Chemistry Reviews, 2003
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Structure Elucidation and Biochemical Characterization of Environmentally Relevant Novel Extradiol Dioxygenases Discovered by a Functional Metagenomics Approach
vipul solanki
mSystems, 2019
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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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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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Dioxygen activation in enzymatic systems and in inorganic models
Constantinos Varotsis
Inorganica Chimica Acta, 1996
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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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NO binding to Mn-substituted homoprotocatechuate 2,3-dioxygenase: relationship to O2 reactivity
Lawrence Que
Journal of Biological Inorganic Chemistry, 2013
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Dioxygenases without Requirement for Cofactors and Their Chemical Model Reaction: Compulsory Order Ternary Complex Mechanism of 1 H -3-Hydroxy-4-oxoquinaldine 2,4-Dioxygenase Involving General Base Catalysis by Histidine 251 and Single-Electron Oxidation of the Substrate Dianion †
Reinhard Kappl
Biochemistry, 2004
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Spectroscopic Investigation of Reduced Protocatechuate 3,4-Dioxygenase: Charge-Induced Alterations in the Active Site Iron Coordination Environment
Mindy Davis
Inorganic Chemistry, 1999
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Iron(iii) complexes of tripodal tetradentate 4N ligands as functional models for catechol dioxygenases: the electronic vs. steric effect on extradiol cleavage
Palaniandavar Mallayan
Dalton Trans., 2014
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An Iron Reservoir to the Catalytic Metal: The Rubredoxin Iron in an Extradiol Dioxygenase
Jiafeng Geng
The Journal of biological chemistry, 2015
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Iron(III) complexes of certain tetradentate phenolate ligands as functional models for catechol dioxygenases
Sonia Sri
Journal of Chemical Sciences, 2006
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Valence tautomerism in catecholato cobalt Bis(phenolate) diamine complexes as models for Enzyme–substrate adducts of catechol dioxygenases
elham safaei
Polyhedron, 2020
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A Structural and Functional Model for Dioxygenases with a 2-His-1-carboxylate Triad
Albert Shteinman
Angewandte Chemie International Edition, 2006
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