Title |
Catalytic robustness and torque generation of the F1-ATPase
|
---|---|
Published in |
Biophysical Reviews, March 2017
|
DOI | 10.1007/s12551-017-0262-x |
Pubmed ID | |
Authors |
Hiroyuki Noji, Hiroshi Ueno, Duncan G. G. McMillan |
Abstract |
The F1-ATPase is the catalytic portion of the FoF1 ATP synthase and acts as a rotary molecular motor when it hydrolyzes ATP. Two decades have passed since the single-molecule rotation assay of F1-ATPase was established. Although several fundamental issues remain elusive, basic properties of F-type ATPases as motor proteins have been well characterized, and a large part of the reaction scheme has been revealed by the combination of extensive structural, biochemical, biophysical, and theoretical studies. This review is intended to provide a concise summary of the fundamental features of F1-ATPases, by use of the well-described model F1 from the thermophilic Bacillus PS3 (TF1). In the last part of this review, we focus on the robustness of the rotary catalysis of F1-ATPase to provide a perspective on the re-designing of novel molecular machines. |
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Student > Bachelor | 17 | 21% |
Student > Ph. D. Student | 13 | 16% |
Researcher | 11 | 14% |
Student > Master | 6 | 7% |
Student > Postgraduate | 4 | 5% |
Other | 10 | 12% |
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Unknown | 25 | 31% |