Ernst-Walter Knapp, Klaus Schulten, and Zan Schulten.
Proton conduction in linear hydrogen-bonded systems.
Chemical Physics, 46:215-229, 1980.
KNAP80
It has been suggested that the hydrophilic side groups of proteins can form hydrogen-bonded conductors that transport protons across biomembranes. Based on previous studies of the proton dynamics in ice, a kinetic model for such proton conductors is developed. The steady-state proton current is evaluated as a function of the pH and voltage difference along the conductor. This electrochemical potential is found to determine the mechanism by which the protons are transported. Under acidic conditions the proton current is inversely proportional to the number of side groups composing the conductor and is determined by the rate of injecting a L-Bjerrum orientation fault into the hydrogen-bonded conductor. For small voltages (<100 mV) an analytical expression for the proton flux is derived.
Download Full Text
The manuscripts available on our site are provided for your personal
use only and may not be retransmitted or redistributed without written
permissions from the paper's publisher and author. You may not upload any
of this site's material to any public server, on-line service, network, or
bulletin board without prior written permission from the publisher and
author. You may not make copies for any commercial purpose. Reproduction
or storage of materials retrieved from this web site is subject to the
U.S. Copyright Act of 1976, Title 17 U.S.C.