Energetic signalling in the control of mitochondrial F1F0 ATP synthase activity in health and disease

The International Journal of Biochemistry & Cell Biology
Gary J GroverDonna Seto-Young

Abstract

The mitochondrial F1F0 ATP synthase is a critical enzyme that works by coupling the proton motive force generated by the electron transport chain via proton transfer through the F0 or proton-pore forming domain of this enzyme to release ATP from the catalytic F1 domain. This enzyme is regulated by calcium, ADP, and inorganic phosphate as well as increased transcription through several pathways. This enzyme is also an ATP hydrolase under ischemic conditions. This "inefficient" hydrolysis of ATP consumes 90% of ATP consumed during ischemia as shown with non-selective ATPase inhibitors oligomycin and Aurovertin B. A benzopyran analog, BMS-199264, selectively inhibits F1F0 ATP hydrolase activity with no effect on ATP synthase activity. BMS-199264 had no effect on ATP before ischemia, but reduced the decline in ATP during ischemia. Selective hydrolase inhibition seen with the small molecule BMS-199264 suggests a conformational change in the F1F0 ATPase enzyme when switching from synthase to hydrolase activity.

References

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Citations

Oct 27, 2009·Cardiovascular Toxicology·Nuno G MachadoPaulo J Oliveira
Dec 17, 2009·Cell Death and Differentiation·T Vanden BergheP Vandenabeele
May 24, 2012·The Journal of Antibiotics·Lyudmila N LysenkovaMaria N Preobrazhenskaya
Apr 29, 2009·Journal of Bioenergetics and Biomembranes·Lesley A Kane, Jennifer E Van Eyk
Sep 1, 2009·Biochimica Et Biophysica Acta·Christos Chinopoulos, Vera Adam-Vizi
Oct 29, 2013·Journal of Pharmacological Sciences·Ryosuke TanakaYasuo Matsumura
Jan 16, 2013·The Journal of Nutritional Biochemistry·Emilie MartinezPatrick Brachet

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