Voltammetry of a "protein on a rope".

Journal article

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. The "tethered" cytochrome c(555)(m) displays remarkably fast electron-transfer kinetics, with an electrochemical exchange rate constant k(0) of 1.4 x 10(4) s(-1). The results show that fast electron transfer is associated with weak interactions: importantly, the tethered cytochrome can explore many different orientations without escaping into solution.

Authors: Baymann, F; Barlow, N; Aubert, C; Schoepp-Cothenet, B; Leroy, G

• Publication status: Published
• Journal: FEBS letters
• Volume: 539
• Issue: 1-3
• Pages: 91-94
• Publication date: 2003-03-01
• DOI: 10.1016/s0014-5793(03)00206-0
• EISSN: 1873-3468
• ISSN: 0014-5793
• Language: English
• Keywords: Amino Acid Sequence; Molecular Sequence Data; Recombinant Proteins; Bacteria; Cytochrome c Group; Electron Transport; Bacterial Proteins; Electrodes; Adsorption; Escherichia coli