Substrate, substrate analogue, and inhibitor interactions with the ferrous active site of catechol 2,3-dioxygenase monitored through XAS studies.
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.
Bertini
I
I
Dipartimento di Chimica, Università di Firenze, Italy.
Briganti
F
F
Mangani
S
S
Nolting
H F
HF
Scozzafava
A
A
D001426:Bacterial Proteins / Q000737:chemistry; D050557:Catechol 2,3-Dioxygenase; D002396:Catechols / Q000737:chemistry; D049308:Dioxygenases; D005296:Ferrous Compounds; D010105:Oxygenases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D016958:Pseudomonas putida / Q000201:enzymology; D013057:Spectrum Analysis; D014965:X-Rays
D001426:Bacterial Proteins; D002396:Catechols; D005296:Ferrous Compounds; D010105:Oxygenases; D049308:Dioxygenases; D050557:Catechol 2,3-Dioxygenase; C034221:catechol