The dithiol reagents phenylarsine oxide (PAO) and dibromobimane (DBrB) have opposite effects on the F₁F_O-ATPase activity. PAO 20% increases ATP hydrolysis at 50 μM when the enzyme activity is activated by the natural cofactor Mg²⁺ and at 150 μM when it is activated by Ca²⁺. The PAO-driven F₁F_O-ATPase activation is reverted to the basal activity by 50 μM dithiothreitol (DTE). Conversely, 300 μM DBrB decreases the F₁F_O-ATPase activity by 25% when activated by Mg²⁺ and by 50% when activated by Ca²⁺. In both cases, the F₁F_O-ATPase inhibition by DBrB is insensitive to DTE. The mitochondrial permeability transition pore (mPTP) formation, related to the Ca²⁺-dependent F₁F_O-ATPase activity, is stimulated by PAO and desensitized by DBrB. Since PAO and DBrB apparently form adducts with different cysteine couples, the results highlight the crucial role of cross-linking of vicinal dithiols on the F₁F_O-ATPase, with (ir)reversible redox states, in the mPTP modulation.

二硫醇试剂苯胂氧化物 (PAO) 和二溴二苯胺 (DBrB) 对 F ₁ F _O -ATPase 活性具有相反的影响。当酶活性被天然辅因子 Mg ²⁺激活时，PAO 20% 增加了 50 μM 的 ATP 水解，而当它被 Ca ²⁺激活时，PAO 20% 增加了 150 μM 。PAO 驱动的 F ₁ F _O -ATPase 激活被 50 μM 二硫苏糖醇 (DTE) 恢复到基础活性。相反，300 μM DBrB在被 Mg ²⁺激活时将 F ₁ F _O -ATPase 活性降低 25%，在被 Ca ²⁺激活时降低 50% 。在这两种情况下，F ₁ F _ODBrB 对 ATP 酶的抑制对 DTE 不敏感。与 Ca ²⁺依赖的 F ₁ F _O -ATPase 活性相关的线粒体通透性转换孔 (mPTP) 的形成受 PAO 刺激并被 DBrB 脱敏。由于 PAO 和 DBrB 显然与不同的半胱氨酸对形成加合物，结果强调了 F ₁ F _O -ATPase上的邻二硫醇交联在 mPTP 调制中的关键作用，具有（非）可逆氧化还原状态。