线粒体 FF-ATP 酶利用二硫键氧化还原状态来调节渗透转移孔。
The mitochondrial FF-ATPase exploits the dithiol redox state to modulate the permeability transition pore.
机构信息
Department of Veterinary Medical Sciences, University of Bologna, Via Tolara di Sopra, 50, Ozzano Emilia, Bologna, 40064, Italy.
Department of Veterinary Medical Sciences, University of Bologna, Via Tolara di Sopra, 50, Ozzano Emilia, Bologna, 40064, Italy.
出版信息
Arch Biochem Biophys. 2021 Nov 15;712:109027. doi: 10.1016/j.abb.2021.109027. Epub 2021 Sep 11.
The dithiol reagents phenylarsine oxide (PAO) and dibromobimane (DBrB) have opposite effects on the FF-ATPase activity. PAO 20% increases ATP hydrolysis at 50 μM when the enzyme activity is activated by the natural cofactor Mg and at 150 μM when it is activated by Ca. The PAO-driven FF-ATPase activation is reverted to the basal activity by 50 μM dithiothreitol (DTE). Conversely, 300 μM DBrB decreases the FF-ATPase activity by 25% when activated by Mg and by 50% when activated by Ca. In both cases, the FF-ATPase inhibition by DBrB is insensitive to DTE. The mitochondrial permeability transition pore (mPTP) formation, related to the Ca-dependent FF-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 FF-ATPase, with (ir)reversible redox states, in the mPTP modulation.
二硫醇试剂苯胂氧（PAO）和二溴双马来酰亚胺（DBrB）对 FF-ATP 酶活性有相反的影响。当酶活性被天然辅因子 Mg 激活时，PAO 在 50μM 时将 ATP 水解增加 20%，而当它被 Ca 激活时增加 150μM。PAO 驱动的 FF-ATP 酶激活被 50μM 二硫苏糖醇（DTE）还原为基础活性。相反，300μM DBrB 在 Mg 激活时使 FF-ATP 酶活性降低 25%，在 Ca 激活时降低 50%。在这两种情况下，DBrB 对 FF-ATP 酶的抑制作用对 DTE 不敏感。与 Ca 依赖性 FF-ATP 酶活性相关的线粒体通透性转换孔（mPTP）形成受 PAO 刺激和 DBrB 脱敏。由于 PAO 和 DBrB 显然与不同的半胱氨酸对形成加合物，因此结果强调了 FF-ATP 酶上相邻二硫键的交联（顺反异构）状态在 mPTP 调节中的关键作用。
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