Voltammetry of a 'protein on a rope'

被引：19

作者：

Baymann, F

Barlow, NL

Aubert, C

Schoepp-Cothenet, B

Leroy, G

Armstrong, FA

机构：

[1] Inorgan Chem Lab, Oxford, England

[2] CNRS, IBSM, F-13402 Marseille 20, France

来源：

FEBS LETTERS | 2003年 / 539卷 / 1-3期

关键词：

cytochrome; voltammetry; electron transfer; Aquifex aeolicus;

D O I：

10.1016/S0014-5793(03)00206-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

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页码：91 / 94

页数：4

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