Visualization of the redox condition in activating cells

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Oxidation is an important biochemical defense mechanism, but it also elicits toxicity; therefore, oxidation must be under strict control. In phagocytotic events in neutrophils, the voltage-gated H+ channel is a key regulator of the production of reactive oxygen species against invading bacteria. In this study, we solved the crystal structure of the cytoplasmic coiled-coil domain of the voltage-gated H+ channel in reduced, oxidized and mutated (Cys to Ser) states. The crystal structures indicated that a pair of Cys residues in the dimeric coiled-coil forms an intersubunit disulfide bond dependent on the redox conditions. Circular dichroism spectroscopy revealed that the disulfide bond increased the thermal stability of the coiled-coil protein. Thus, we revealed that the voltage-gated H+ channel has a redox-sensor in the cytoplasmic domain. We also tried to monitor the redox condition using the coiled-coil in cells.