Inactivation of beef heart mitochondrial F₁‐ATPase by the 2′,3′‐dialdehyde derivatives of adenine nucleotides

Abstract

Beef fietzrf mitochondri~~ Ft-ATPase was i~~~t~vat~ by the 2" ,3 '-dialdehyde derivatives of ATP, ADP and AMP {ATP, oADP, oAMP). In the absence of Mg2+, i~a~t~~~on resuIWl from the binding Of 1 mol nuekotide analog per active unit of Fi. The most efficient andog was oADP, followed by oAMP and oATP, Complete inactivsxtion was correlated with the binding; of about 11 moi ["%]oADPr'mol Ft, After ~orr~~ti~r~ for non-specifk labeling, the ~~~~ber of sp~ifi~~~ly bound fi4C]oADP was 2-3 mol per mol Fi. By S~S-polyacryl~m~~~ gel eiectrophoresis, [i4C]oADP was found to bind covalently mainly to the LY and fl subunits. In the presence of Mga', oATP behaved 8s a substrate and was sfowly hydrolyzed.~ucl~~de sites in the Ft sector of m~tocb~n-

ATP Depletion via Mitochondrial F1F0Complex by Lethal Factor is an Early Event inB. Anthracis-Induced Sudden Cell Death

“… 12 An independent study showed that oxidized ATP also binds irreversibly to both α and β subunits of mitochondrial F 1 ATPase and decreases its activity. 13 Here we show that after internalization, LF localizes to mitochondria and interacts with F 1 F 0 complex proteins including, subunits β and γ, resulting in increased ATPase activity and depletion of cellular ATP, which is a critical early event in LT-induced sudden (pyroptotic) cell death.…”