The mitochondrial F1FO-ATPase exploits the dithiol redox state to modulate the permeability transition pore
نویسندگان
چکیده
The dithiol reagents phenylarsine oxide (PAO) and dibromobimane (DBrB) have opposite effects on the F 1 O -ATPase activity. PAO 20% increases ATP hydrolysis at 50 μM when enzyme activity is activated by natural cofactor Mg 2+ 150 it Ca . PAO-driven activation reverted to basal dithiothreitol (DTE). Conversely, 300 DBrB decreases 25% 50% In both cases, inhibition insensitive DTE. mitochondrial permeability transition pore (mPTP) formation, related -dependent activity, stimulated desensitized DBrB. Since apparently form adducts with different cysteine couples, results highlight crucial role of cross-linking vicinal dithiols -ATPase, (ir)reversible redox states, in mPTP modulation. • inhibited DBrB, respectively. reversible state sensitive PAO. irreversible
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ژورنال
عنوان ژورنال: Archives of Biochemistry and Biophysics
سال: 2021
ISSN: ['1096-0384', '0003-9861']
DOI: https://doi.org/10.1016/j.abb.2021.109027