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Physiological Reviews, Vol. 83, No. 2, April 2003, pp. 475-579; 10.1152/physrev.00028.2002.
Copyright ©2003 by the American Physiological Society
Department of Molecular Biophysics and Physiology, Rush Presbyterian St. Luke's Medical Center, Chicago, Illinois
Decoursey, Thomas E.
Voltage-Gated Proton Channels and Other Proton Transfer
Pathways. Physiol. Rev. 83: 475-579, 2003.
Proton channels exist in a wide
variety of membrane proteins where they transport protons rapidly and
efficiently. Usually the proton pathway is formed mainly by water
molecules present in the protein, but its function is regulated by
titratable groups on critical amino acid residues in the pathway. All
proton channels conduct protons by a hydrogen-bonded chain
mechanism in which the proton hops from one water or titratable group
to the next. Voltage-gated proton channels represent a specific
subset of proton channels that have voltage- and time-dependent
gating like other ion channels. However, they differ from most ion
channels in their extraordinarily high selectivity, tiny conductance,
strong temperature and deuterium isotope effects on conductance and
gating kinetics, and insensitivity to block by steric occlusion. Gating
of H+ channels is regulated tightly by pH and voltage,
ensuring that they open only when the electrochemical gradient is
outward. Thus they function to extrude acid from cells. H+
channels are expressed in many cells. During the respiratory burst in
phagocytes, H+ current compensates for electron extrusion
by NADPH oxidase. Most evidence indicates that the H+
channel is not part of the NADPH oxidase complex, but rather is a
distinct and as yet unidentified molecule.
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