Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase

By R. Yasuda, H. Noji, Masasuke Yoshida, K. Kinosita, H. Itoh. Nature, 2001

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The vacuolar (H+)-ATPases — nature's most versatile proton pumps (2002, background): “The F-ATPases are believed to function through a rotary mechanis”
Single metal nanoparticles: optical detection, spectroscopy and applications (2011, methodology): “However, the highspeed images of a single metal sphere recorded by Yasuda et al revealed that the rotation is actually stochastic in nature and a 120◦ step consists of substeps, each only taking a fraction of a millisecond [321].”
Cell and molecular mechanics of biological materials (2003, neutral): “When ATP is supplied, the F 1 -ATPase rotates 120° stepwise, with one ATP molecule hydrolysed per ste”
Movements of the ε‐subunit during catalysis and activation in single membrane‐bound H+‐ATP synthase (2005, background): “Rotation of the g-subunit has been observed with molecule ensembles (Duncan et al, 1995; Sabbert et al, 1996) and with single immobilized F1 subcomplexes (Noji et al, 1997; Yasuda et al, 2001 ).”
SINGLE-PARTICLE TRACKING (2009, background): “Another class of motor proteins are the rotary motors of flagellae and ATP synthase [78,79].”
Molecular mechanisms of photosynthesis (2002, background): “Other experiments have established that the rotary motion takes place in 120 degree jumps (Adachi et al., 2000; Yasuda et al., 2001; Adachi et al., 2007).”