Dual Oxidase (Duox) is a member of the NADPH oxidase (NOX) family that is responsible for the production of H2O2 in the thyroid and immune cells. It has been shown that Ca2+ plays a crucial role in the activation of Duox, but little is known about its Ca2+ binding properties. In order to better understand these properties, we isolated the EF-hand domain of Duox (EFD) using recombinant protein technology. EFD binds specifically to Ca2+, and its ANS binding shows that a hydrophobic patch is exposed upon Ca2+ binding. The ITC measurements reveal the exothermic and endothermic reactions in the low and high Ca2+ concentrations, respectively, which implies a macroscopically negative cooperative binding. Currently, we are generating EFD mutants/constructs to investigate structural changes upon Ca2+ binding.

Characterization of EF-hand domain of Dual Oxidase

245th National Meeting (2013)

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