Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation

Abstract

F1-ATPase is a rotary molecular motor in which unidirectional rotation of the central γ subunit is powered by ATP hydrolysis in three catalytic sites arranged 120° apart around γ. 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… (More)
DOI: 10.1038/nsmb721

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