Experimental and theoretical affinity studies of substituted phenols to chlorocatechol 1,2-dioxygenases: A step toward the comprehension of inhibitor/substrate binding to intradiol dioxygenases

Autor:	Marta Ferraroni, Fabrizio Briganti, Andrea Scozzafava, L. A. Golovleva, A.M. Chernykh, M. P. Kolomytseva
Rok vydání:	2010
Předmět:	Chemistry Stereochemistry Process Chemistry and Technology Van der Waals surface Bioengineering Biochemistry Catalysis Active center chemistry.chemical_compound Rhodococcus opacus Partial charge symbols.namesake Deprotonation symbols Reactivity (chemistry) Enzyme kinetics Phenols
Zdroj:	Journal of Molecular Catalysis B: Enzymatic. 64:53-59
ISSN:	1381-1177
DOI:	10.1016/j.molcatb.2010.02.001
Popis:	The inhibition kinetics of 4- and 3-chlorocatechol 1,2-dioxygenases from Rhodococcus opacus 1CP were investigated using 14 different substituted phenols. The obtained experimental data were analyzed against experimental (pKa) and theoretical reactivity parameters of the phenols calculated by semi-empirical AM1 method (DPE, EHOMO, charge on oxygen atom of the reactive hydroxyl group, van der Waals surface areas and partial charges of substituents on aromatic ring). From these comparisons it appears that the main factor determining the inhibitors binding in the active center of these enzymes is the deprotonation ability of their reactive hydroxyl group. The analysis also allowed to detect, in 3-CCD, enzyme factors influencing on the interactions with the investigated phenols. Some correlations between the calculated van der Waals surface areas as well as the partial charges of substituents on the aromatic ring of the phenols and their inhibition effect on the enzymes were found.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::4433d0449994725aa7bd82ece30fe3bd https://doi.org/10.1016/j.molcatb.2010.02.001 Zobrazit plný text záznamu Full Text from ScienceDirect