Electrostatic origin of the mechanochemical rotary mechanism and the catalytic dwell of F1-ATPase.

ABSTRACT: Understanding the nature of energy transduction in life processes requires a quantitative description of the energetics of the conversion of ATP to ADP by ATPases. Previous attempts to do so have provided an interesting insight but could not account for the rotary mechanism by a nonphenomenological structure/energy description. In particular it has been very challenging to account for the observations of the 80° and 40° rotational substates, without any prior information about such states in the simulation procedure. Here we use a coarse-grained model of F1-ATPase and generate, without the adjustment of phenomenological parameters, a structure-based free energy landscape that reproduces the energetics of the mechanochemical process. It is found that the landscape along the relevant rotary

SUBMITTER: Mukherjee S 

PROVIDER: S-EPMC3251122 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature