Aliphatic and aromatic inhibitors binding to the active site of catechol 2,3‐dioxygenase from Pseudomonas putida mt‐2

FEBS Letters

Bertini, Ivano¹  Briganti, Fabrizio¹  Scozzafava, Andrea¹ 

[1] Laboratorio di Chimica Inorganica e Bioinorganica, Dipartimento di Chimica, Università di Firenze, Via Gino Capponi 7, 1-50121 Florence, Italy

关键词: Catechol;    Dioxygenase;    Extradiol cleavage;    Pseudomonas putida;    C2;    30;    Catechol 2;    3-dioxygenase;    EPR;    Electron Paramagnetic resonance;    NMR Nuclear Magnetic Resonance;    XAS;    X-ray Absorption Spectroscopy;   

DOI  :  10.1016/0014-5793(94)80606-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The interaction of different classes of inhibitors with the extradiol cleaving catechol 2,3-dioxygenase from Pseudomonas putida mt-2 was monitored by longitudinal and transverse proton relaxation measurements as well as by kinetic activity studies in order to characterize the type of interaction of such inhibitors with the active site of the enzyme. The average distances of the inhibitors from the catalytic iron(II) ion have been estimated from the ¹H longitudinal relaxation rates. Phenols and aliphatic ketones appear to be coordinated to the iron(II) ion in the active site.

【 授权许可】

Unknown