These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: Chemomechanical coupling mechanism of F(1)-ATPase: catalysis and torque generation. Author: Watanabe R, Noji H. Journal: FEBS Lett; 2013 Apr 17; 587(8):1030-5. PubMed ID: 23395605. Abstract: F1-ATPase (F1), a rotary motor protein driven by ATP hydrolysis, is unique with respect to its high efficiency and reversibility in converting chemical energy into mechanical work. Single-molecule studies have improved our understanding about the energy-conversion mechanism of F1 and the chemomechanical-coupling scheme under ATP hydrolysis conditions. A novel single-molecule technique was recently established to estimate the free-energy change of F1 during catalysis at elementary-step resolution, advancing our understanding about the energy-conversion mechanism of ATP hydrolysis and synthesis. The energy conversion mechanism of F1 elucidated from single-molecule studies provides us with important insights into the operating principles underlying molecular motors.[Abstract] [Full Text] [Related] [New Search]