期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 114, 期 19, 页码 4960-4965出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1700801114
关键词
FoF1-ATP synthase; chemiosmotic coupling theory; ATPase; proton motive force; electrochemical potential
资金
- Japan Society for the Promotion of Science
- ATP synthesis Regulation Project
- Grants-in-Aid for Scientific Research [17H05717, 15K07014] Funding Source: KAKEN
FoF1-ATP synthase (FoF1) couples H+ flow in Fo domain and ATP synthesis/hydrolysis in F1 domain through rotation of the central rotor shaft, and the H+/ATP ratio is crucial to understand the coupling mechanism and energy yield in cells. Although H+/ATP ratio of the perfectly coupling enzyme can be predicted from the copy number of catalytic beta subunits and that of H+ binding c subunits as c/beta, the actual H+/ATP ratio can vary depending on coupling efficiency. Here, we report actual H+/ATP ratio of thermophilic Bacillus FoF1, whose c/beta is 10/3. Proteoliposomes reconstituted with the FoF1 were energized with.pH and.. by the acid-base transition and by valinomycin-mediated diffusion potential of K+ under various [ATP]/([ADP].[Pi]) conditions, and the initial rate of ATP synthesis/ hydrolysis was measured. Analyses of thermodynamically equilibrated states, where net ATP synthesis/hydrolysis is zero, show linear correlation between the chemical potential of ATP synthesis/hydrolysis and the proton motive force, giving the slope of the linear function, that is, H+/ATP ratio, 3.3 +/- 0.1. This value agrees well with the c/beta ratio. Thus, chemomechanical coupling between Fo and F1 is perfect.
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