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Voltammetry of a "protein on a rope".

Abstract:

A periplasmic electron-transfer protein, cytochrome c(555)(m) from Aquifex aeolicus contains a 62-residue N-terminal extension by which it is anchored to the membrane--most probably via a thioester bond to its N-terminal cysteine. This linker can act as a "rope" to tether the protein close to its reaction partners. Mimicking this principle, a recombinant cytochrome c(555)(m), expressed in Escherichia coli, has been attached covalently to a gold electrode modified with 6-mercaptohexan-1-ol. Th...

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Publication status:
Published

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Journal:
FEBS letters
Volume:
539
Issue:
1-3
Pages:
91-94
Publication date:
2003-03-01
DOI:
EISSN:
1873-3468
ISSN:
0014-5793
Source identifiers:
32333
Language:
English
Keywords:
Pubs id:
pubs:32333
UUID:
uuid:c4113e3b-8ebb-47a5-9822-bf4422f1a9b8
Local pid:
pubs:32333
Deposit date:
2013-11-17

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