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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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Journal:
Biochimica et biophysica acta
Volume:
1757
Issue:
3
Pages:
206-214
Publication date:
2006-03-01
DOI:
ISSN:
0006-3002
Source identifiers:
160168
Language:
English
Keywords:
Pubs id:
pubs:160168
UUID:
uuid:c17177f8-3f51-4a97-a422-e65dab0e9d9a
Local pid:
pubs:160168
Deposit date:
2013-11-16

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