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Substrate, substrate analogue, and inhibitor interactions with the ferrous active site of catechol 2,3‐dioxygenase monitored through XAS studies
Author(s) -
Bertini Ivano,
Briganti Fabrizio,
Mangani Stefano,
Nolting Hans F.,
Scozzafava Andrea
Publication year - 1994
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 - 10.1016/0014-5793(94)00771-3
Subject(s) - catechol , substrate (aquarium) , active site , x ray absorption spectroscopy , chemistry , dioxygenase , ferrous , binding site , stereochemistry , enzyme , biochemistry , absorption spectroscopy , organic chemistry , biology , ecology , physics , quantum mechanics
The interactions of catechol (substrate), 2‐hydroxy‐pyridine‐ N ‐oxide (substrate analogue) and 2‐bromophenol (inhibitor) with the extradiol cleaving catechol‐2,3‐dioxygenase from Pseudomonas putida mt‐2 have been monitored through X‐ray absorption spectroscopy (XAS). The analysis of the data provides details about the mode of coordination of the substrate and of the inhibitors to the active site of the enzyme.