The 3 × 120° rotary mechanism of Paracoccus denitrificans F(1)-ATPase is different from that of the bacterial and mitochondrial F(1)-ATPases

The rotation of Paracoccus denitrificans F(1)-ATPase (PdF(1)) was studied using single-molecule microscopy. At all concentrations of adenosine triphosphate (ATP) or a slowly hydrolyzable ATP analog (ATPγS), above or below K(m), PdF(1) showed three dwells per turn, each separated by 120°. Analysis of...

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Vydáno v:Proc Natl Acad Sci U S A
Hlavní autoři: Zarco-Zavala, Mariel, Watanabe, Ryo, McMillan, Duncan G. G., Suzuki, Toshiharu, Ueno, Hiroshi, Mendoza-Hoffmann, Francisco, García-Trejo, José J., Noji, Hiroyuki
Médium: Artigo
Jazyk:Inglês
Vydáno: National Academy of Sciences 2020
Témata:
Biological Sciences
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC7703542/
https://ncbi.nlm.nih.gov/pubmed/33168750
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.2003163117
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