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J Biol Chem, Vol. 274, Issue 45, 31792-31796, November 5, 1999

Acid-labile ATP and/or ADP/P_i Binding to the Tetraprotomeric Form of Na/K-ATPase Accompanying Catalytic Phosphorylation-Dephosphorylation Cycle

Takeshi Yokoyama, Shunji Kaya, Kazuhiro Abe, Kazuya Taniguchi, Tsuyoshi Katoh^¶, Michio Yazawa^¶, Yutaro Hayashi, and Sven Mårdh^**

From  Biological Chemistry and ^¶ Bioorganic Chemistry, Division of Chemistry, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan, the  Department of Biochemistry, Kyorin University School of Medicine, Mitaka 181-1611, Japan, and the ^** Department of Biomedicine and Surgery, Faculty of Health Sciences, Linköping University, Linköping S-581 85, Sweden

The Na/K-ATPase has been shown to bind 1 and 0.5 mol of ³²P/mol of -chain in the presence [-³²P]ATP and [-³²P]ATP, respectively, accompanied by a maximum accumulation of 0.5 mol of ADP-sensitive phosphoenzyme (NaE1P) and potassium-sensitive phosphoenzyme (E2P). The former accumulation was followed by the slow constant liberation of P_i, but the latter was accompanied with a rapid ~0.25 mol of acid-labile P_i burst. The rubidium (potassium congener)-occluded enzyme (~1.7 mol of rubidium/mol of -chain) completely lost rubidium on the addition of sodium + magnesium. Further addition of ~100 µM [-³²P]ATP and [-³²P]ATP, both induced 0.5 mol of ³²P-ATP binding to the enzyme and caused accumulation of ~1 mol of rubidium/mol of -chain, accompanied by a rapid ~0.5 mol of P_i burst with no detectable phosphoenzyme under steady state conditions. Electron microscopy of rotary-shadowed soluble and membrane-bound Na/K-ATPases and an antibody-Na/K-ATPase complex, indicated the presence of tetraprotomeric structures ()₄. These and other data suggest that Na/K-ATP hydrolysis occurs via four parallel paths, the sequential appearance of (NaE1P:E·ATP)₂, (E2P:E·ATP:E2P:E·ADP/P_i), and (KE2:E·ADP/P_i)₂, each of which has been previously referred to as NaE1P, E2P, and KE2, respectively.

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