ArticleProceedings of the National Academy of Sciences of the United States of America2011
Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 18 citations in OpenAlex.
- Molecular Mechanism of ATP Hydrolysis in an ABC Transporter.ACS central science · 2018Article
- Dynamic mechanisms driving conformational conversions of the β and ε subunits involved in rotational catalysis of FProceedings of the Japan Academy. Series B, Physical and biological sciences · 2017Review
- Characterization of the thermal and photoinduced reactions of photochromic spiropyrans in aqueous solution.The journal of physical chemistry. B · 2013Article
- Rate of hydrolysis in ATP synthase is fine-tuned by α-subunit motif controlling active site conformation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Why nature really chose phosphate.Quarterly reviews of biophysics · 2013Review
- Electrostatic origin of the mechanochemical rotary mechanism and the catalytic dwell of F1-ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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 stepwise scans and several models of the nucleotide-bound active site, some of the most important conformational changes were traced toward direction of synthesis. Interestingly, as the active site geometry progresses toward the ATP-favoring tight binding site, at both of these TSs, a dramatic increase in barrier heights is observed for the reverse direction, i.e., hydrolysis of ATP. This change could indicate a "ratchet" mechanism for the enzyme to ensure efficacy of ATP synthesis by shifting residue conformation and thus locking access to the crucial TSs.
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