Premium
XAS characterization of the active sites of novel intradiol ring‐cleaving dioxygenases: hydroxyquinol and chlorocatechol dioxygenases
Author(s) -
Briganti Fabrizio,
Mangani Stefano,
Pedocchi Luca,
Scozzafava Andrea,
Golovleva Ludmila A,
Jadan Andrea P,
Solyanikova Inna P
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00884-9
Subject(s) - dioxygenase , chemistry , substrate (aquarium) , x ray absorption spectroscopy , double bond , stereochemistry , active site , adduct , absorption spectroscopy , enzyme , organic chemistry , physics , quantum mechanics , oceanography , geology
The intradiol cleaving dioxygenases hydroxyquinol 1,2‐dioxygenase (HQ1,2O) from Nocardiodes simplex 3E, chlorocatechol 1,2‐dioxygenase (ClC1,2O) from Rhodococcus erythropolis 1CP, and their anaerobic substrate adducts (hydroxyquinol‐HQ1,2O and 4‐chlorocatechol‐ClC1,2O) have been characterized through X‐ray absorption spectroscopy. In both enzymes the iron(III) is pentacoordinated and the distance distribution inside the Fe(III) first coordination shell is close to that already found in the extensively characterized protocatechuate 3,4‐dioxygenase. The coordination number and the bond lengths are not significantly affected by the substrate binding. Therefore it is confirmed that the displacement of a protein donor upon substrate binding has to be considered a general step valid for all intradiol dioxygenases.