| Range |
CF0F1 200sec^-1 :MF0F1 100sec^-1 sec^-1
|
| Organism |
Various |
| Reference |
Petersen J, Förster K, Turina P, Gräber P. Comparison of the H+/ATP ratios of the H+-ATP synthases from yeast and from chloroplast. Proc Natl Acad Sci U S A. 2012 Jul 10 109(28):11150-5. doi: 10.1073/pnas.1202799109. p.11151 left column 2nd paragraphPubMed ID22733773
|
| Primary Source |
[17] Förster K, et al. (2010) Proton transport coupled ATP synthesis by the purified yeast H+-ATP synthase in proteoliposomes. Biochim Biophys Acta 1797: 1828–1837. [21] Schmidt G, Gräber P (1985) The rate of ATP-synthesis by reconstituted CF0F1 liposomes. Biochim Biophys Acta 808 :46–51. [22] Grotjohann I, Gräber P (2002) The H+-ATPase from chloroplasts: effect of different reconstitution procedures on ATP synthesis activity and on phosphate dependence of ATP synthesis. Biochim Biophys Acta 1556: 208–216.PubMed ID20691145, 12460678
|
| Method |
"Liposomes from phosphatidylcholine/phosphatidic
acid were prepared, and either the chloroplast or the mitochondrial
enzyme was reconstituted into the liposome membrane.
When these proteoliposomes were energized by acid–base transitions
they catalyzed rates of ATP synthesis up to 200 s^-1 with
CF0F1 (primary sources 21, 22) and 100 s^-1 with MF0F1 (primary source 17) (i.e., they displayed
synthesis activities in the physiological range)." |
| Comments |
CF0F1 from chloroplasts [primary sources 21, 22] MF0F1 from yeast mitochondria [primary source 17] |
| Entered by |
Uri M |
| ID |
111520 |