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

Journal of Molecular Catalysis B: Enzymatic

Volumn 64, Issue 1-2, 2010, Pages 53-59

  Kolomytseva, M P ^a   Ferraroni, M ^b   Chernykh, A M ^a   Scozzafava, A ^b   Briganti, F ^b   Golovleva, L A ^a  

^a SKRYABIN INSTITUTE OF BIOCHEMISTRY AND PHYSIOLOGY OF MICROORGANISMS   (Russian Federation)

^b UNIVERSITY OF FLORENCE   (Italy)

Author keywords

Chlorocatechol 1,2 dioxygenase; Enzyme kinetics; Molecular orbital calculations; Quantitative structure activity relationship (QSAR); Substrate analogue reactivity

Indexed keywords

ACTIVE CENTER; AM 1 METHOD; AROMATIC RINGS; CHLOROCATECHOL; DIOXYGENASES; EXPERIMENTAL DATA; HYDROXYL GROUPS; INHIBITION EFFECT; INHIBITION KINETICS; INHIBITOR/SUBSTRATE; MOLECULAR ORBITAL CALCULATIONS; OXYGEN ATOM; PARTIAL CHARGES; REACTIVITY PARAMETERS; RHODOCOCCUS OPACUS; SEMI-EMPIRICAL; STRUCTURE/ACTIVITY RELATIONSHIP; SUBSTITUTED PHENOL; SURFACE AREA; VAN DER WAALS;

CATALYSTS; ENZYME INHIBITION; ENZYME KINETICS; ENZYMES; MOLECULAR MODELING; MOLECULAR ORBITALS; OXYGEN; VAN DER WAALS FORCES;

PHENOLS;

CHLOROCATECHOL 1,2 DIOXGENASE; DIOXYGENASE; HYDROXYL GROUP; INTRADIOL DIOXYGENASE; PHENOL DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CHEMICAL STRUCTURE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME BINDING; ENZYME INHIBITOR COMPLEX; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; EXPERIMENTAL STUDY; HYDROPHILICITY; HYDROPHOBICITY; SURFACE CHARGE;

RHODOCOCCUS OPACUS;

EID: 77951498139     PISSN: 13811177     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcatb.2010.02.001     Document Type: Article

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