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Stepping rotation of F(1)-ATPase with one, two, or three altered catalytic sites that bind ATP only slowly.
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Catalytic site occupancy during ATP synthase catalysis.
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Pause and rotation of F(1)-ATPase during catalysis.
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Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis.
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Bi-site catalysis in F1-ATPase: does it exist?
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Chemical physics. Single-molecule spectroscopy comes of age.
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Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.
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The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution.
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The renaissance of fluorescence resonance energy transfer.
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