Standard Gibbs free energies of ATP synthesis on lipid vesicles

Range for extra-vesicular pH=8.05 36±3: for extra-vesicular pH=8.45 37±2 kJ/mol
Organism Spinach Spinacia oleracea
Reference Turina, Paola, Dietrich Samoray, and Peter Gräber. "H+/ATP ratio of proton transport-coupled ATP synthesis and hydrolysis catalysed by CF0F1—liposomes." The EMBO journal 22.3 (2003): 418-426. abstract & p.423 left column bottom paragraph & right column top paragraphPubMed ID12554643
Method Reconstitution of the spinach chloroplast F0F1 ATP synthase on lipid vesicles. ATP synthesis is coupled to a luciferase assay.
Comments Abstract:"The standard Gibbs free energies of ATP synthesis were determined to be 37 ± 2 kJ/mol at pH 8.45 and 36 ± 3 kJ/mol at pH 8.05." p.423 left column bottom paragraph:"The y-axis intercepts [of fig.5] give the standard Gibbs free energies ?Gp°' (see equation 4), with the values of 37 ± 2 and 36 ± 3 kJ/mol for pHout = 8.45 and pHout = 8.05, respectively. The error limits are the standard deviations of the slope and the intercept of the linear regression analysis. When the corrected ?pH (eq) data (see Table III) were used for this analysis, [investigators] obtained values of 4.0 ± 0.3 for the H+/ATP ratio and ?Gp°' = 37 ± 3 kJ/mol at pHout = 8.45 and 4.2 ± 0.3 for the H+/ATP ratio and ?Gp°' = 37 ± 2 kJ/mol at pHout = 8.05, which is, within error limits, the same as with the uncorrected data."
Entered by Uri M
ID 111503