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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 |
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| Hlavní autoři: | , , , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
2020
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| Témata: | |
| 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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