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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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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Kinetic and spectroscopic studies of cobalt- and manganese-substituted extradiol-cleaving homoprotocatechuate 2,3-dioxygenases
Jay Fielding
2013
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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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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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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 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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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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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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Manganese(II)-Dependent Extradiol-Cleaving Catechol Dioxygenase from Arthrobacter globiformis CM-2
Lawrence Que
Biochemistry, 1996
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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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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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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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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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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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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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Functional models for catechol dioxygenases: Iron(III) complexes of cis-facially coordinating linear 3N ligands
Marappan Velusamy
Journal of Inorganic Biochemistry, 2005
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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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Catecholate and phenolate iron complexes as models for the dioxygenases
Lawrence Que
Journal of the American Chemical Society, 1982
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Iron(III) Complexes with Meridional Ligands as Functional Models of Intradiol-Cleaving Catechol Dioxygenases
József Kaizer
Inorganic Chemistry, 2013
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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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Spectroscopic studies of the catechol dioxygenases
Lawrence Que
Journal of Chemical Education, 1985
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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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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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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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Five-coordinate MII-semiquinonate (M = Fe, Mn, Co) complexes: reactivity models of the catechol dioxygenases
Charles Riordan
Chem. Commun., 2014
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Higher Metal−Ligand Coordination in the Catalytic Site of Cobalt-Substituted Thermoanaerobacter brockii Alcohol Dehydrogenase Lowers the Barrier for Enzyme Catalysis
Oren Bogin
Biochemistry, 2004
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Iron(III) complexes of N2O and N3O donor ligands as functional models for catechol dioxygenase enzymes: ether oxygen coordination tunes the regioselectivity and reactivity
Palaniandavar Mallayan
Dalton Transactions, 2011
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Novel Iron(III) Complexes of Tripodal and Linear Tetradentate Bis(phenolate) Ligands: Close Relevance to Intradiol-Cleaving Catechol Dioxygenases
Sonia Sri
Inorganic Chemistry, 2003
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Characterization of the Cobaltochelatase CbiXL
Kirsty McLean
Journal of Biological Chemistry, 2003
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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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Crystal structure of BphC, a halotolerant catechol dioxygenase
vipul solanki
2019
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Dioxygenase models. Crystal structures of N,N'-(1,2-phenylene)bis(salicylideniminato)iron(III) and .mu.-(1,4-benzenediolato-O,O')-bis[N,N'-ethylenebis(salicylideniminato)iron(III)]
Lawrence Que
Inorganic Chemistry, 1982
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Cloning, overexpression, purification, characterization and structural modelling of a metabolically active Fe2+ dependent 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (CpsA) from Bacillus cereus strain AOA-CPS_1
Oladipupo A. AREGBESOLA
International Journal of Biological Macromolecules, 2020
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