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Title: Fast state detection in F₁-ATPase rotation enhanced by theory of mixed states and external torque
Authors: Le, Luan Q.
Volkán-Kacsó, Sándor
Keywords: Engineering::Materials
Issue Date: 2021
Source: Le, L. Q. & Volkán-Kacsó, S. (2021). Fast state detection in F₁-ATPase rotation enhanced by theory of mixed states and external torque. New Journal of Physics, 23(11), 113030-.
Journal: New Journal of Physics
Abstract: During brief 120 degrees transitions between long catalytic dwells, single F-1-ATPase molecules exhibit angular jumps that vary with rotation angles. Using the angular jump profile enables the detection of fast states in the mechano-chemical scheme of the enzyme, states that are difficult to capture from single-molecule trajectories due to the fluctuations of the imaging nanoprobe. In a previous work, a short-lived, three occupancy state was postulated from a multi-state, probabilistic theory to explain the mean angular jump profile. An assumption in the theory was that the 'mixing' of chemical states is negligible during jumps. In a mixing event, two subsequent angular positions recorded by the imaging apparatus belong to two different chemical states of the motor enzyme due to fast reactions within a recording frame. In this paper, we provide an enhanced method for the detection of fast states. On one hand, we show using Langevin simulations that state mixing leads to faster mean angular jump, shifting up the profile. Consequently, the improved method provides a correction to the angular position and lifetime of the postulated three-occupancy metastable state. On the other hand, we show that when F-1-ATPase is subject to torques opposing rotation in hydrolysis direction, the torques shift down the dwell angles without affecting the angle-dependent reaction rates. The torques improve detection capability for the fast state by increasing dwell times which is made evident by the flattening of the mean angular jump profile within 40 degrees-60 degrees from the catalytic dwell. In the three-occupancy state release of ADP occurs in concert with the binding of ATP to a different site in the F-1-ATPase. Similarly, in the full ATP synthase when torques are created by the proton gradient in the F-O region, the release of the product ATP is presumably accelerated by the binding of ADP to a different site in the F-1 domain.
ISSN: 1367-2630
DOI: 10.1088/1367-2630/ac33f4
Rights: © 2021 The Author(s). Published by IOP Publishing Ltd on behalf of the Institute of Physics and Deutsche Physikalische Gesellschaft. Original content from this work may be used under the terms of the Creative Commons Attribution 4.0 licence.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:MSE Journal Articles

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