Journal article
A functionally inactive, cold-stabilized form of the Escherichia coli F1Fo ATP synthase.
- Abstract:
-
An unusual effect of temperature on the ATPase activity of E. coli F1Fo ATP synthase has been investigated. The rate of ATP hydrolysis by the isolated enzyme, previously kept on ice, showed a lag phase when measured at 15 degrees C, but not at 37 degrees C. A pre-incubation of the enzyme at room temperature for 5 min completely eliminated the lag phase, and resulted in a higher steady-state rate. Similar results were obtained using the isolated enzyme after incorporation into liposomes. The i...
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- Publisher copy:
- 10.1016/j.bbabio.2006.02.011
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Bibliographic Details
- Journal:
- Biochimica et biophysica acta
- Volume:
- 1757
- Issue:
- 3
- Pages:
- 206-214
- Publication date:
- 2006-03-05
- DOI:
- ISSN:
-
0006-3002
- URN:
-
uuid:c17177f8-3f51-4a97-a422-e65dab0e9d9a
- Source identifiers:
-
160168
- Local pid:
- pubs:160168
Item Description
Terms of use
- Copyright date:
- 2006
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