A Caltech Library Service

Evaluation of P. denitrificans F1-ATPase Rotary Motion using Automated Methods to Detect Hidden States

Suiter, Nathan M. and Bettencourt, Jordan M. and Volkán-Kacsó, Sándor and Matute, Ricardo A. (2021) Evaluation of P. denitrificans F1-ATPase Rotary Motion using Automated Methods to Detect Hidden States. Biophysical Journal, 120 (3, Supp. 1). 172a. ISSN 0006-3495. doi:10.1016/j.bpj.2020.11.1212.

Full text is not posted in this repository. Consult Related URLs below.

Use this Persistent URL to link to this item:


F-ATPase is a rotary motor enzyme with the biological function of synthesizing ATP, the “fuel molecule” of cells. A subsystem of F-ATPase, F1-ATPase, functions in reverse: it hydrolyses ATP into ADP and inorganic phosphate. During this process, the rotation of F1-ATPase's shaft-like rotor is driven by chemical free energy. Samples of paracoccus denitrificans F1-ATPase are studied in single-molecule imaging experiments while the enzyme undergoes ATP synthesis. This single-molecule experiment is performed through the use of a 40 nanometer gold nano-probe used to record rotation angles at a microsecond temporal resolution. The biomotor enzyme experiences rotary motion during the hydrolysis of ATP, and periodically transitions between various states (angular dwells) in a step-like manner. The substeps observed in other species of F1-ATPase appear to be absent in the paracoccus denitrificans species, so a goal of our work is to use a previous multi-state theory for the angle-dependent velocity to detect any “hidden” substeps with too short a lifespan to be seen in the experimental trajectories. Additionally, the Brownian motion of the probe prohibits analysis of the possible state configuration of F1-ATPase through direct observation. Due to this, we have developed an automated method utilizing the enzyme's rotary progression as well as likelihood theorems to separate dwell and transitional states within single molecule trajectories. The method thereby allows an analysis of the state model of experimental results using calculations based on the existing theory.

Item Type:Article
Related URLs:
URLURL TypeDescription
Matute, Ricardo A.0000-0002-0644-3799
Additional Information:© 2021 Biophysical Society.
Issue or Number:3, Supp. 1
Record Number:CaltechAUTHORS:20210217-104426134
Persistent URL:
Official Citation:Nathan M. Suiter, Jordan M. Bettencourt, Sandor Volkan-Kacso, Ricardo A. Matute, Evaluation of P. denitrificans F1-ATPase Rotary Motion using Automated Methods to Detect Hidden States, Biophysical Journal, Volume 120, Issue 3, Supplement 1, 2021, Page 172a, ISSN 0006-3495, (
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:108089
Deposited By: Tony Diaz
Deposited On:18 Feb 2021 19:13
Last Modified:16 Nov 2021 19:08

Repository Staff Only: item control page