Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase.

ABSTRACT: In a majority of living organisms, FoF1 ATP synthase performs the fundamental process of ATP synthesis. Despite the simple net reaction formula, ADP+Pi→ATP+H2O, the detailed step-by-step mechanism of the reaction yet remains to be resolved owing to the complexity of this multisubunit enzyme. Based on quantum mechanical computations using recent high resolution X-ray structures, we propose that during ATP synthesis the enzyme first prepares the inorganic phosphate for the γP-OADP bond-forming step via a double-proton transfer. At this step, the highly conserved αS344 side chain plays a catalytic role. The reaction thereafter progresses through another transition state (TS) having a planar ion configuration to finally form ATP. These two TSs are concluded crucial for ATP synthesis. Using ste

SUBMITTER: Beke-Somfai T 

PROVIDER: S-EPMC3064393 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature