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To study how hydrolysis reactions produce mechanical rotation, we observed rotation under an optical microscope to see which of the three sites bound and released a fluorescent ATP analog. Assuming that the analog mimics authentic ATP, the following scheme emerges: (i) in the ATP-waiting state, one site, dictated by the orientation of gamma, is empty, whereas the other two bind a nucleotide; (ii) ATP binding to the empty site drives an approximately 80 degrees rotation of gamma; (iii) this triggers a reaction(s), hydrolysis and/or phosphate release, but not ADP release in the site that bound ATP one step earlier; (iv) completion of this reaction induces further approximately 40 degrees rotation."}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380290617685186567","@type":"Researcher","foaf:name":[{"@value":"Takayuki Nishizaka"}]},{"@id":"https://cir.nii.ac.jp/crid/1382262944564878469","@type":"Researcher","foaf:name":[{"@value":"Kazuhiro Oiwa"}]},{"@id":"https://cir.nii.ac.jp/crid/1382262944564878464","@type":"Researcher","foaf:name":[{"@value":"Hiroyuki Noji"}]},{"@id":"https://cir.nii.ac.jp/crid/1382262944564878468","@type":"Researcher","foaf:name":[{"@value":"Shigeki Kimura"}]},{"@id":"https://cir.nii.ac.jp/crid/1382262944564878466","@type":"Researcher","foaf:name":[{"@value":"Eiro 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