TY - JOUR
T1 - Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging
AU - Adachi, Kengo
AU - Yasuda, Ryohei
AU - Noji, Hiroyuki
AU - Itoh, Hiroyasu
AU - Harada, Yoshie
AU - Yoshida, Masasuke
AU - Kinosita, Kazuhiko
PY - 2000/6/20
Y1 - 2000/6/20
N2 - Orientation dependence of single-fluorophore intensity was exploited in order to videotape conformational changes in a protein machine in real time. The fluorophore Cy3 attached to the central subunit of F1-ATPase revealed that the subunit rotates in the molecule in discrete 120°steps and that each step is driven by the hydrolysis of one ATP molecule. These results, unlike those from the previous study under a frictional load, show that the 120° stepping is a genuine property of this molecular motor. The data also show that the rate of ATP binding is insensitive to the load exerted on the rotor subunit.
AB - Orientation dependence of single-fluorophore intensity was exploited in order to videotape conformational changes in a protein machine in real time. The fluorophore Cy3 attached to the central subunit of F1-ATPase revealed that the subunit rotates in the molecule in discrete 120°steps and that each step is driven by the hydrolysis of one ATP molecule. These results, unlike those from the previous study under a frictional load, show that the 120° stepping is a genuine property of this molecular motor. The data also show that the rate of ATP binding is insensitive to the load exerted on the rotor subunit.
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U2 - 10.1073/pnas.120174297
DO - 10.1073/pnas.120174297
M3 - Article
C2 - 10840052
AN - SCOPUS:0034690806
SN - 0027-8424
VL - 97
SP - 7243
EP - 7247
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 13
ER -