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

Abstract:

The rotary motor F(1)-ATPase from the thermophilic Bacillus PS3 (TF(1)) is one of the best-studied of all molecular machines. F(1)-ATPase is the part of the enzyme F(1)F(O)-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 F(1)-ATPase from Escherichia coli (EF(1...

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Publication status:
Published

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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
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Physics
Pilizota, T More by this author
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Journal:
Philosophical transactions of the Royal Society of London. Series B, Biological sciences
Volume:
368
Issue:
1611
Pages:
20120023
Publication date:
2013-02-05
DOI:
EISSN:
1471-2970
ISSN:
0962-8436
URN:
uuid:39ebe44a-55bd-407e-bfa7-3903e99231d9
Source identifiers:
369824
Local pid:
pubs:369824

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