Functional properties of Na,K-ATPase, and their structural implications, as detected with biophysical techniques.
A full understanding of the molecular mechanism of ion transport and energetics of the Na,K-ATPase will require both structural and functional data. During recent years biophysical methods have provided a number of important pieces of information on ion binding and release and the charge transfer process. This allows the formulation of kinetic models of the transport process. Although a breakthrough has not been obtained due to the lack of detailed knowledge on the three-dimensional structure with a resolution high enough to identify the ion-binding sites and the transport pathway, the functional information has structural implications that create constraints on possible mechanisms of active transport. Here we describe briefly contributions of some biophysical methods to our conceptual understanding of the ion transport process.
Department of Biology, University of Konstanz, Fach M635, 78457 Konstanz, Germany.
H J
HJ
Apell
S J
SJ
Karlish
D011487:Protein Conformation; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry
D000254:Sodium-Potassium-Exchanging ATPase