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., Briganti, F., Mangani, S., Nolting, H.F., Scozzafava, A. (1994). Substrate, Substrate-analog, and Inhibitor Interactions With the Ferrous Active-site of Catechol 2,3-dioxygenase Monitored Through Xas Studies. FEBS LETTERS, 350(2-3), 207-212 [10.1016/0014-5793(94)00771-3].
Substrate, Substrate-analog, and Inhibitor Interactions With the Ferrous Active-site of Catechol 2,3-dioxygenase Monitored Through Xas Studies
Mangani, Stefano;
1994-01-01
Abstract
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.
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