Background: Three catalytically charged residues of F 1 -ATPase, P-loop lysine, general base, and arginine finger, are thought to be indispensable for catalysis. Results: Alanine-substituted mutants of the catalytic residues of F 1 -ATPase drove rotations.
Conclusion:The catalytic residues contribute to efficient catalysis but are not indispensable to chemo-mechanical energy coupling of F 1 -ATPase. Significance: The chemo-mechanical coupling mechanism of F 1 -ATPase is far more robust than previously thought.
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