Cargando…
Angle-dependent rotation velocity consistent with ADP release in bacterial F( 1 )-ATPase
A model-based method is used to extract a short-lived state in the rotation kinetics of the F(1)-ATPase of a bacterial species, Paracoccus denitrificans (PdF1). Imaged as a single molecule, PdF1 takes large 120( ø ) steps during it rotation. The apparent lack of further substeps in the trajectories...
Autores principales: | Suiter, Nathan, Volkán-Kacsó, Sándor |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10433373/ https://www.ncbi.nlm.nih.gov/pubmed/37602322 http://dx.doi.org/10.3389/fmolb.2023.1184249 |
Ejemplares similares
-
Physical pictures of rotation mechanisms of F(1)- and V(1)-ATPases: Leading roles of translational, configurational entropy of water
por: Yasuda, Satoshi, et al.
Publicado: (2023) -
Rotary mechanism of V/A-ATPases—how is ATP hydrolysis converted into a mechanical step rotation in rotary ATPases?
por: Yokoyama, Ken
Publicado: (2023) -
F(1)-ATPase Rotary Mechanism: Interpreting Results of Diverse Experimental Modes With an Elastic Coupling Theory
por: Volkán-Kacsó, Sándor, et al.
Publicado: (2022) -
Modulation of the H(+)/ATP coupling ratio by ADP and ATP as a possible regulatory feature in the F-type ATP synthases
por: Turina, Paola
Publicado: (2022) -
The Universally Conserved ATPase YchF Regulates Translation of Leaderless mRNA in Response to Stress Conditions
por: Landwehr, Victoria, et al.
Publicado: (2021)