1999年7月
The gamma-subunit rotation and torque generation in F-1-ATPase from wild-type or uncoupled mutant Escherichia coli
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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- 巻
- 96
- 号
- 14
- 開始ページ
- 7780
- 終了ページ
- 7784
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1073/pnas.96.14.7780
- 出版者・発行元
- NATL ACAD SCIENCES
The rotation of the gamma-subunit has been included in the binding-change mechanism of ATP synthesis/hydrolysis by the proton ATP synthase (FOF1), The Escherichia coli ATP synthase was engineered for rotation studies such that its ATP hydrolysis and synthesis activity is similar to that of wild type. A fluorescently labeled actin filament connected to the gamma-subunit of the F-1 sector rotated on addition of ATP, This progress enabled us to analyze the gamma M23K (the gamma-subunit Met-23 replaced by Lys) mutant, which is defective in energy coupling between catalysis and proton translocation. We found that the F-1 sector produced essentially the same frictional torque, regardless of the mutation. These results suggest that the gamma M23K mutant is defective in the transformation of the mechanical work into proton translocation or vice versa.
- リンク情報
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- DOI
- https://doi.org/10.1073/pnas.96.14.7780
- CiNii Articles
- http://ci.nii.ac.jp/naid/80011239993
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/10393898
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000081342100035&DestApp=WOS_CPL
- ID情報
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- DOI : 10.1073/pnas.96.14.7780
- ISSN : 0027-8424
- CiNii Articles ID : 80011239993
- PubMed ID : 10393898
- Web of Science ID : WOS:000081342100035