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The mitochondrial F1FO-ATPase exploits the dithiol redox state to modulate the permeability transition pore
Archives of Biochemistry and Biophysics ( IF 3.8 ) Pub Date : 2021-09-11 , DOI: 10.1016/j.abb.2021.109027
Cristina Algieri 1 , Fabiana Trombetti 1 , Alessandra Pagliarani 1 , Vittoria Ventrella 1 , Salvatore Nesci 1
Affiliation  

The dithiol reagents phenylarsine oxide (PAO) and dibromobimane (DBrB) have opposite effects on the F1FO-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 F1FO-ATPase activation is reverted to the basal activity by 50 μM dithiothreitol (DTE). Conversely, 300 μM DBrB decreases the F1FO-ATPase activity by 25% when activated by Mg2+ and by 50% when activated by Ca2+. In both cases, the F1FO-ATPase inhibition by DBrB is insensitive to DTE. The mitochondrial permeability transition pore (mPTP) formation, related to the Ca2+-dependent F1FO-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 F1FO-ATPase, with (ir)reversible redox states, in the mPTP modulation.



中文翻译:

线粒体 F1FO-ATPase 利用二硫醇氧化还原状态来调节渗透性转换孔

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。

更新日期:2021-09-16
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