title: F1F0-ATP synthases of alkaliphilic bacteria: lessons from their adaptations.
abstract: This review focuses on the ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values>10. At such pH values the protonmotive force, which is posited to provide the energetic driving force for ATP synthesis, is too low to account for the ATP synthesis observed. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient. Several anticipated solutions to this bioenergetic conundrum have been ruled out. Although the transmembrane sodium motive force is high under alkaline conditions, respiratory alkaliphilic bacteria do not use Na+- instead of H+-coupled ATP synthases. Nor do they offset the adverse pH gradient with a compensatory increase in the transmembrane electrical potential component of the protonmotive force. Moreover, studies of ATP synthase rotors indicate that alkaliphiles cannot fully resolve the energetic problem by using an ATP synthase with a large number of c-subunits in the synthase rotor ring. Increased attention now focuses on delocalized gradients near the membrane surface and H+ transfers to ATP synthases via membrane-associated microcircuits between the H+ pumping complexes and synthases. Microcircuits likely depend upon proximity of pumps and synthases, specific membrane properties and specific adaptations of the participating enzyme complexes. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components.
authors.affiliation: Department of Pharmacology and Systems Therapeutics, Mount Sinai School of Medicine, New York, NY 10029, USA. david.hicks@mssm.edu
authors.forename: David B
authors.initials: DB
authors.lastname: Hicks
authors.forename: Jun
authors.initials: J
authors.lastname: Liu
authors.forename: Makoto
authors.initials: M
authors.lastname: Fujisawa
authors.forename: Terry A
authors.initials: TA
authors.lastname: Krulwich
mesh_terms: D000222:Adaptation, Physiological; D000255:Adenosine Triphosphate / Q000096:biosynthesis; D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology; D001419:Bacteria / Q000201:enzymology*; D004734:Energy Metabolism; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D010766:Phosphorylation; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000502:physiology*
chemical_list: D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases