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| Cross-linking and electron microscopy studies of the structure and functioning of the Escherichia coli ATP synthase |
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| Author(s): Capaldi RA, Schulenberg B, Murray J, Aggeler R |
| Source: JOURNAL OF EXPERIMENTAL BIOLOGY Volume: 203 Issue: 1 Pages: 29-33 Published: JAN 2000 |
| Times Cited: 39 References: 43 |
| Abstract: ATP synthase, also called F1Fo-ATPase, catalyzes the synthesis of ATP during oxidative phosphorylation. The enzyme is reversible and is able to use ATP to drive a proton gradient for transport purposes. Our work has focused on the enzyme from Escherichia coli (ECF1Fo), We have used a combination of methods to study this enzyme, including electron microscopy and chemical cross-linking. The utility of these two approaches in particular, and the important insights they give into the structure and mechanism of the ATP synthase, are reviewed. |
| Document Type: Article |
| Language: English |
| Reprint Address: Capaldi, RA (reprint author), Univ Oregon, Inst Mol Biol, Eugene, OR 97403 USA |
Addresses:
1. Univ Oregon, Inst Mol Biol, Eugene, OR 97403 USA |
| Publisher: COMPANY OF BIOLOGISTS LTD, BIDDER BUILDING CAMBRIDGE COMMERCIAL PARK COWLEY RD, CAMBRIDGE CB4 4DL, CAMBS, ENGLAND |
| Subject Category: Biology |
| IDS Number: 277ZG |
| ISSN: 0022-0949 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |