Ontology highlight
ABSTRACT:
SUBMITTER: Hirono-Hara Y
PROVIDER: S-EPMC555477 | biostudies-literature | 2005 Mar
REPOSITORIES: biostudies-literature
Hirono-Hara Yoko Y Ishizuka Koji K Kinosita Kazuhiko K Yoshida Masasuke M Noji Hiroyuki H
Proceedings of the National Academy of Sciences of the United States of America 20050309 12
A rotary motor F(1), a catalytic part of ATP synthase, makes a 120 degrees step rotation driven by hydrolysis of one ATP, which consists of 80 degrees and 40 degrees substeps initiated by ATP binding and probably by ADP and/or P(i) dissociation, respectively. During active rotations, F(1) spontaneously fails in ADP release and pauses after a 80 degrees substep, which is called the ADP-inhibited form. In the present work, we found that, when pushed >+40 degrees with magnetic tweezers, the pausing ...[more]