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• W3104359558 abstract "The voltage-dependent anion channel (VDAC) is the most abundant protein in the mitochondrial outer membrane and an archetypical β-barrel channel. Here, we study the effects of temperature on VDAC channels reconstituted in planar lipid membranes at the single- and multichannel levels within the 20°C to 40°C range. The temperature dependence of conductance measured on a single channel in 1 M KCl shows an increase characterized by a 10°C temperature coefficient Q10 = 1.22 ± 0.02, which exceeds that of the bathing electrolyte solution conductivity, Q10 = 1.17 ± 0.01. The rates of voltage-induced channel transition between the open and closed states measured on multichannel membranes also show statistically significant increases, with temperatures that are consistent with activation energy barriers of ∼10 ± 3 kcal/mol. At the same time, the gating thermodynamics, as characterized by the gating charge and voltage of equipartitioning, does not display any measurable temperature dependence. The two parameters stay within 3.2 ± 0.2 elementary charges and 30 ± 2 mV, respectively. Thus, whereas the channel kinetics, specifically its conductance and rates of gating response to voltage steps, demonstrates a clear increase with temperature, the conformational voltage-dependent equilibria are virtually insensitive to temperature. These results, which may be a general feature of β-barrel channel gating, suggest either an entropy-driven gating mechanism or a role for enthalpy-entropy compensation." @default.
• W3104359558 created "2020-11-23" @default.
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• W3104359558 date "2020-12-01" @default.
• W3104359558 modified "2023-10-16" @default.
• W3104359558 title "VDAC Gating Thermodynamics, but Not Gating Kinetics, Are Virtually Temperature Independent" @default.
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• W3104359558 doi "https://doi.org/10.1016/j.bpj.2020.10.039" @default.
• W3104359558 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7822735" @default.
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