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Substrate, substrate analogue, and inhibitor interactions with the ferrous active site of catechol 2,3-dioxygenase monitored through XAS studies.

作者信息

Bertini I, Briganti F, Mangani S, Nolting H F, Scozzafava A

机构信息

Dipartimento di Chimica, Università di Firenze, Italy.

出版信息

FEBS Lett. 1994 Aug 22;350(2-3):207-12. doi: 10.1016/0014-5793(94)00771-3.

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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