Abstract
ATP synthase (F1F0-ATPase), consisting of a water-soluble F1 portion and a transmembrane FO portion, is present in bacterial cytoplasmic membranes and the inner membranes of mitochondria and chloroplasts. This enzyme plays a central role in biological energy transduction. F1F0-ATPase is bifunctional, being involved in ATP synthesis and hydrolysis. When bacteria are subjected to specific environmental challenges, F1F0-ATPase changes its operation to overcome the challenges. F1F0-ATPase synthesizes ATP using energy released from proton movement in oxidative phosphorylation under aerobic conditions at a near-neutral pH. This enzyme exports protons coupled with ATP hydrolysis as a reverse reaction in some specific environments. Recent research has indicated that F1F0-ATPase plays an important role in bacterial survival in markedly acidic environments. In this chapter, the roles of F1F0-ATPase in bacteria subjected to marked acidic stress are discussed.
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Acknowledgements
The author would like to express thanks to Hiroshi Kobayashi (Chiba University) for his valuable suggestions.
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Sun, Y. (2016). F1F0-ATPase Functions Under Markedly Acidic Conditions in Bacteria. In: Chakraborti, S., Dhalla, N. (eds) Regulation of Ca2+-ATPases,V-ATPases and F-ATPases. Advances in Biochemistry in Health and Disease, vol 14. Springer, Cham. https://doi.org/10.1007/978-3-319-24780-9_22
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DOI: https://doi.org/10.1007/978-3-319-24780-9_22
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