Title | Date | PubMed ID |
Binding pockets and permeation channels for dioxygen through cofactorless 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase in association with its natural substrate, 3-hydroxy-2-methylquinolin-4(1H)-one. A perspective from molecular dynamics simulations. | 2014 Jun | 24934672 |
Thermodynamic analysis of denaturant-induced unfolding of HodC69S protein supports a three-state mechanism. | 2008 Jul 8 | 18549245 |
Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rü61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily. | 2007 May 1 | 17565176 |
Stability, unfolding, and structural changes of cofactor-free 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase. | 2007 Apr 10 | 17371045 |
Dioxygenases without requirement for cofactors: identification of amino acid residues involved in substrate binding and catalysis, and testing for rate-limiting steps in the reaction of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase. | 2005 Nov | 16187153 |
Dioxygenases without requirement for cofactors and their chemical model reaction: compulsory order ternary complex mechanism of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase involving general base catalysis by histidine 251 and single-electron oxidation of the substrate dianion. | 2004 Nov 16 | 15533053 |
Bacterial 2,4-dioxygenases: new members of the alpha/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases. | 1999 Sep | 10482514 |
2,4-dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Rü61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1. | 1996 Sep 15 | 8856057 |