Global stability of an α-ketoglutarate-dependent dioxygenase (TauD) and its related complexes.

ABSTRACT:

Background

TauD is a nonheme iron(II) and α-ketoglutarate (αKG) dependent dioxygenase, and a member of a broader family of enzymes that oxidatively decarboxylate αKG to succinate and carbon dioxide thereby activating O₂ to perform a range of oxidation reactions. However before O₂ activation can occur, these enzymes bind both substrate and cofactor in an effective manner. Here the thermodynamics associated with substrate and cofactor binding to FeTauD are explored.

Methods

Thermal denaturation of TauD and its enzyme-taurine, enzyme-αKG, and enzyme-taurine-αKG complexes are explored using circular dichroism (CD) spectroscopy and differential scanning calorimetry (DSC).

Results

Taurine binding is endothermic (+26kcal/mol) and entropically driven tha

SUBMITTER: Henderson KL 

PROVIDER: S-EPMC5453726 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature