pH homeostasis and bioenergetic work in alkalophiles.
A Na+/H+ antiporter catalyses coupled Na+ extrusion and H+ uptake across the membranes of extremely alkalophilic bacilli. This exchange is electrogenic, with H+ translocated inward greater than Na+ extruded. It is energized by the delta chi 2 component of the delta mu H+ that is established during primary proton pumping by the alkalophile respiratory chain complexes. These complexes abound in the membranes of extreme alkalophiles. Combined activity of the respiratory chain, the antiporter, and solute transport systems that are coupled to Na+ re-entry, allow the alkalophiles to maintain a cytoplasmic pH that is several pH units more acidic than optimal external pH values for growth. There is no compelling evidence for a specific and necessary role for any ion other than sodium in pH homeostasis, and although there is very high cytoplasmic buffering capacity in the alkaline range, active mechanisms for pH homeostasis are crucial. Energization of the antiporter as well as the proton translocating F1F0-ATPase that catalyses ATP synthesis in the extreme alkalophiles must accommodate the problem of the low net delta mu H+ and the very low concentrations of protons, per se, in the external medium. This problem is by-passed by other bioenergetic work functions, such as solute uptake or motility, that utilize sodium ions for energy-coupling in the place of protons.
Krulwich
T A
TA
Department of Biochemistry, Mount Sinai School of Medicine, City University of New York, N.Y.
Guffanti
A A
AA
Seto-Young
D
D
D001407:Bacillus / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D006706:Homeostasis; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008954:Models, Biological; D012964:Sodium / Q000378:metabolism*; D017923:Sodium-Hydrogen Exchangers
D002352:Carrier Proteins; D017923:Sodium-Hydrogen Exchangers; D012964:Sodium