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• W2647490639 abstract "The mitochondrial F-ATPase can be activated either by the classical cofactor Mg2+ or, with lower efficiency, by Ca2+. The latter may play a role when calcium concentration rises in mitochondria, a condition associated with cascade events leading to cell death. Common and distinctive features of these differently activated mitochondrial ATPases were pointed out in swine heart mitochondria. When Ca2+ replaces the natural cofactor Mg2+, the enzyme responsiveness to the transmembrane electrochemical gradient and to the classical F-ATPase inhibitors DCCD and oligomycin as well as the oligomycin sensitivity loss by thiol oxidation, are maintained. Consistently, the two mitochondrial ATPases apparently share the F1FO complex basic structure and mechanism. Peculiar cation-dependent properties, which may affect the F1 catalytic mechanism and/or the FO proton binding site features, may be linked to a different physiological role of the mitochondrial Ca-activated F-ATPase with respect to the Mg-activated F-ATPase." @default.
• W2647490639 created "2017-06-30" @default.
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• W2647490639 date "2017-09-01" @default.
• W2647490639 modified "2023-10-18" @default.
• W2647490639 title "Kinetic properties of the mitochondrial F 1 F O -ATPase activity elicited by Ca 2+ in replacement of Mg 2+" @default.
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• W2647490639 doi "https://doi.org/10.1016/j.biochi.2017.06.013" @default.
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