Chemo-mechanical coupling in F1-ATPaSe revealed by catalytic site occupancy during catalysis

Rieko Shimo-Kon, Eiro Muneyuki, Hiroshi Sakai, Kengo Adachi, Masasuke Yoshida, Kazuhiko Kinosita

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    43 Citations (Scopus)

    Abstract

    F1-ATPase is a rotary molecular motor in which the central γ subunit rotates inside a cylinder made of α3β 3 subunits. To clarify how ATP hydrolysis in three catalytic sites cooperate to drive rotation, we measured the site occupancy, the number of catalytic sites occupied by a nucleotide, while assessing the hydrolysis activity under identical conditions. The results show hitherto unsettled timings of ADP and phosphate releases: starting with ATP binding to a catalytic site at an ATP-waiting γ angle defined as 0°, phosphate is released at -200°, and ADP is released during quick rotation between 240° and 320° that is initiated by binding of a third ATP. The site occupancy remains two except for a brief moment after the ATP binding, but the third vacant site can bind a medium nucleotide weakly.

    Original languageEnglish
    Pages (from-to)1227-1236
    Number of pages10
    JournalBiophysical Journal
    Volume98
    Issue number7
    DOIs
    Publication statusPublished - 2010 Apr 7

    ASJC Scopus subject areas

    • Biophysics

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    Shimo-Kon, R., Muneyuki, E., Sakai, H., Adachi, K., Yoshida, M., & Kinosita, K. (2010). Chemo-mechanical coupling in F1-ATPaSe revealed by catalytic site occupancy during catalysis. Biophysical Journal, 98(7), 1227-1236. https://doi.org/10.1016/j.bpj.2009.11.050