Premium
Mechanism of Proton Pumping by Plant Plasma Membrane H + ‐ATPase
Author(s) -
PALMGREN M. G.,
BUCHPEDERSEN M. J.,
MØLLER A. L.
Publication year - 2003
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2003.tb07159.x
Subject(s) - atpase , chemistry , proton , p type atpase , proton pump , mutagenesis , membrane , transmembrane protein , mechanism (biology) , biophysics , biochemistry , enzyme , mutation , biology , physics , receptor , gene , quantum mechanics
A bstract : The mechanism of proton pumping by P‐type plasma membrane H + ‐ATPases is not well clarified. Site‐directed mutagenesis studies suggest that Asp684, situated in transmembrane segment M6, is involved in coordination of proton(s) in plant plasma membrane H + ‐ATPase. This hypothesis is supported by atomic models of H + ‐ATPases built on the basis of the crystal structure of the related SERCA1a Ca 2+ ‐ATPase. However, more biochemical, genetic, and structural studies are required before we will be able to understand the nature of the proton binding site(s) in P‐type H + ‐ATPases and the mechanism of action of these pumps.