Is Ca2+-ATPase a water pump?
The mechanism of free energy coupling in active transport is discussed with special reference to the sarcoplasmic reticulum Ca2+-ATPase. In the current working schemes for cation transport ATPases, free energy transduction is nearly always based on enzyme conformational changes. The principal objective of the present article is to examine whether recent experimental results on Ca2+-ATPase may in fact be better explained by assuming the existence of a direct chemiosmotic process. In the scheme proposed, free energy transduction between ATP and calcium is based on a transfer of solvation water between the acylphosphate bond and the bound calcium ions.
D001665:Binding Sites; D001693:Biological Transport, Active; D001834:Body Water / Q000378:metabolism; D002118:Calcium / Q000378:metabolism; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008954:Models, Biological
D000252:Calcium-Transporting ATPases; D002118:Calcium