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High-resolution single-molecule characterization of the enzymatic states in Escherichia coli F1-ATPase

Abstract:

The rotary motor F1-ATPase from the thermophilic Bacillus PS3 (TF1) is one of the best-studied of all molecular machines. F1-ATPase is the part of the enzyme F1FO-ATP synthase that is responsible for generating most of the ATP in living cells. Single-molecule experiments have provided a detailed understanding of how ATP hydrolysis and synthesis are coupled to internal rotation within the motor. In this work, we present evidence that mesophilic F1-ATPase from Escherichia coli (EF1) is governed...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1098/rstb.2012.0023

Authors


Bilyard, T More by this author
Nakanishi-Matsui, M More by this author
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Institution:
University of Oxford
Division:
MPLS
Department:
Physics
Subgroup:
Condensed Matter Physics
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ORCID:
0000-0002-2156-0221
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Publisher:
Royal Society Publisher's website
Journal:
Philosophical Transactions B: Biological Sciences Journal website
Volume:
368
Issue:
1611
Article number:
20120023
Publication date:
2013-02-05
DOI:
EISSN:
1471-2970
ISSN:
0962-8436
Pmid:
23267177
Pubs id:
pubs:369824
UUID:
uuid:8a3119c0-f077-4137-98e6-92603074c4f6
Source identifiers:
369824
Local pid:
pubs:369824
Language:
English
Keywords:

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