Deciphering Intrinsic Inter-subunit Couplings that Lead to Sequential Hydrolysis of F₁-ATPase Ring.

ABSTRACT: Rotary sequential hydrolysis of the metabolic machine F₁-ATPase is a prominent manifestation of high coordination among multiple chemical sites in ring-shaped molecular machines, and it is also functionally essential for F₁ to tightly couple chemical reactions and central γ-shaft rotation. High-speed AFM experiments have identified that sequential hydrolysis is maintained in the F₁ stator ring even in the absence of the γ-rotor. To explore the origins of intrinsic sequential performance, we computationally investigated essential inter-subunit couplings on the hexameric ring of mitochondrial and bacterial F₁. We first reproduced in stochastic Monte Carlo simulations the experimentally determined sequential hydrolysis schemes by kinetically imposin

SUBMITTER: Dai L 

PROVIDER: S-EPMC5627347 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature