Mechanism of proton transport by plant plasma membrane proton ATPases.
The mechanism of proton translocation by P-type proton ATPases is poorly defined. Asp684 in transmembrane segment M6 of the Arabidopsis thaliana AHA2 plasma membrane P-type proton pump is suggested to act as an essential proton acceptor during proton translocation. Arg655 in transmembrane segment M5 seems to be involved in this proton translocation too, but in contrast to Asp684, is not essential for transport. Asp684 may participate in defining the E(1) proton-binding site, which could possibly exist as a hydronium ion coordination center. A model of proton translocation of AHA2 involving the side chains of amino acids Asp684 and Arg655 is discussed.
Buch-Pedersen
M J
MJ
Department of Plant Biology, Royal Veterinary and Agricultural University, Thorvaldsensvej 40, opg. 8, 5 sal, 1871 Frederiksberg, Denmark. mob@kvl.dk
Palmgren
M G
MG
D017360:Arabidopsis / Q000201:enzymology*; D029681:Arabidopsis Proteins / Q000378:metabolism; D001120:Arginine; D001665:Binding Sites; D001692:Biological Transport; D002462:Cell Membrane / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D009492:Neurospora crassa / Q000201:enzymology; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000145:classification / Q000378:metabolism*; D011522:Protons
D029681:Arabidopsis Proteins; D011522:Protons; D001120:Arginine; D006180:Proton-Translocating ATPases