Ion channel enzyme in an oscillating electric field.
To explain the electrical activation of several membrane ATPases, an electroconformational coupling (ECC) model has previously been proposed. The model explained many features of experimental data but failed to reproduce a window of the field intensity for the stimulated activity. It is shown here that if the affinities of the ion for the two conformational states of the transporter (one with binding site on the left side and the other on the right side of the membrane) are dependent on the electric field, the field-dependent transport can exhibit the observed window. The transporter may be described as a channel enzyme which opens to one side of the membrane at a time. It retains the energy-transducing ability of the earlier ECC models. Analysis of the channel enzyme in terms of the Michaelis-Menten kinetics has been done. The model reproduced the amplitude window for the electric field-induced cation pumping by (Na,K)-ATPase.
Markin
V S
VS
Department of Biochemistry, University of Minnesota College of Biological Sciences, St. Paul 55108.
Liu
D
D
Gimsa
J
J
Strobel
R
R
Rosenberg
M D
MD
Tsong
T Y
TY
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D004553:Electric Conductivity; D004789:Enzyme Activation; D004912:Erythrocytes / Q000201:enzymology; D006801:Humans; D007473:Ion Channels / Q000201:enzymology*; D008954:Models, Biological; D012413:Rubidium / Q000378:metabolism
D007473:Ion Channels; D000251:Adenosine Triphosphatases; D012413:Rubidium