The author reviews the molecular properties of Na
+, K
+-ATPase not only to elucidate the reaction sequence of the enzyme, but also to obtain a better understanding of the mechanism of energy transduction. It is shown that the reaction sequence which had been proposed mainly from phosphorylation kinetics has now been proven by the direct measurment of dynamic fluorescence changes during the hydrolysis of ATP. The formation of MgNaE
1 ATP and the transition of NaE
1P to E
2P accompany the largest fluorescence changes in both the intrinsic and the extrinsic probes, respectively. These findings seem to be a useful step for understanding the mechanism of energy transduction in Na
+, K
+-ATPase.
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