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J Biol Chem, Vol. 274, Issue 9, 5701-5706, February 26, 1999

Cross-linking of Two  Subunits in the Closed Conformation in F₁-ATPase

From the Research Laboratory of Resources Utilization, Tokyo Institute of Technology, 4259 Nagatsuta, Yokohama 226, Japan

In the crystal structure of mitochondrial F₁-ATPase, two  subunits with a bound Mg-nucleotide are in "closed" conformations, whereas the third  subunit without bound nucleotide is in an "open" conformation. In this "CCO" (-closed -closed -open) conformational state, Ile-390s of the two closed  subunits, even though they are separated by an intervening  subunit, have a direct contact. We replaced the equivalent Ile of the ₃₃ subcomplex of thermophilic F₁-ATPase with Cys and observed the formation of the - cross-link through a disulfide bond. The analysis of conditions required for the cross-link formation indicates that: (i) F₁-ATPase takes the CCO conformation when two catalytic sites are filled with Mg-nucleotide, (ii) intermediate(s) with the CCO conformation are generated during catalytic cycle, (iii) the Mg-ADP inhibited form is in the CCO conformation, and (iv) F₁-ATPase dwells in conformational state(s) other than CCO when only one (or none) of catalytic sites is filled by Mg-nucleotide or when catalytic sites are filled by Mg²⁺-free nucleotide. The ₃₃ subcomplex containing the - cross-link retained the activity of uni-site catalysis but lost that of multiple catalytic turnover, suggesting that open-closed transition of  subunits is required for the rotation of  subunit but not for hydrolysis of a single ATP.

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