Journal article
Single molecule measurements of F1-ATPase reveal an interdependence between the power stroke and the dwell duration
- Abstract:
- Increases in the power stroke and dwell durations of single molecules of Escherichia coli F1-ATPase were measured in response to viscous loads applied to the motor and inhibition of ATP hydrolysis. The load was varied using different sizes of gold nanorods attached to the rotating γ subunit and/or by increasing the viscosity of the medium using PEG-400, a noncompetitive inhibitor of ATPase activity. Conditions that increase the duration of the power stroke were found to cause 20-fold increases in the length of the dwell. These results suggest that the order of hydrolysis, product release, and substrate binding may change as the result of external load on the motor or inhibition of hydrolysis.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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- Files:
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(Preview, Accepted manuscript, pdf, 1.3MB, Terms of use)
-
- Publisher copy:
- 10.1021/bi9008215
Authors
- Publisher:
- American Chemical Society
- Journal:
- Biochemistry More from this journal
- Volume:
- 48
- Issue:
- 33
- Pages:
- 7979-7985
- Publication date:
- 2009-08-03
- Acceptance date:
- 2009-07-15
- DOI:
- EISSN:
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1520-4995
- ISSN:
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0006-2960
- Language:
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English
- Keywords:
- Pubs id:
-
pubs:154468
- UUID:
-
uuid:27c7209d-2d45-43b5-b544-36ced2c56250
- Local pid:
-
pubs:154468
- Source identifiers:
-
154468
- Deposit date:
-
2013-11-16
Terms of use
- Copyright holder:
- American Chemical Society
- Copyright date:
- 2009
- Rights statement:
- © 2009 American Chemical Society.
- Notes:
- This is the accepted manuscript version of the article. The final version is available online from the American Chemical Society at: https://doi.org/10.1021/bi9008215
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