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Inhibitory Mg-ADP—Fluoroaluminate Complexes Bound to Catalytic Sites of F1-ATPases: Are They Ground-State or Transition-State Analogs?

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Abstract

Schemes are proposed for coupling sequential opening and closing the three catalytic sites of F1 to rotation of the γ subunit during ATP synthesis and hydrolysis catalyzed by the FoF1-ATP synthase. A prominent feature of the proposed mechanisms is that the transition state during ATP synthesis is formed when a catalytic site is in the process of closing and that the transition state during ATP hydrolysis is formed when a catalytic site is in the process of opening. The unusual kinetics of formation of Mg-ADP—fluoroaluminate complexes in one or two catalytic sites of nucleotide-depleted MF1 and wild-type and mutant α3β3γ subcomplexes of TF1 are also reviewed. From these considerations, it is concluded that Mg-ADP—fluoroaluminate complexes formed at catalytic sites of isolated F1-ATPases or F1 in membrane-bound FoF1 are ground-state analogs.

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Authors and Affiliations

  1. Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, California, 92093-0506

    William S. Allison, Huimiao Ren & Chao Dou

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  1. William S. Allison
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  2. Huimiao Ren
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  3. Chao Dou
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Allison, W.S., Ren, H. & Dou, C. Inhibitory Mg-ADP—Fluoroaluminate Complexes Bound to Catalytic Sites of F1-ATPases: Are They Ground-State or Transition-State Analogs?. J Bioenerg Biomembr 32, 531–538 (2000). https://doi.org/10.1023/A:1005677310791

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