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https://hdl.handle.net/2440/38890
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Type: | Journal article |
Title: | Probing the stability of the disulfide radical intermediate of thioredoxin using direct electrochemistry |
Author: | Johnson, D. Polyak, S. Wallace, J. Martin, L. |
Citation: | International Journal of Peptide Research and Therapeutics, 2003; 10(5-6):495-500 |
Publisher: | Springer Netherlands |
Issue Date: | 2003 |
ISSN: | 1573-3149 1573-3904 |
Statement of Responsibility: | Daniel L. Johnson, Steven W. Polyak, John C. Wallace and Lisandra L. Martin |
Abstract: | Thioredoxin, a redox active disulfide protein, has been specifically immobilized at a modified gold electrode. The thioredoxin is uniquely oriented relative to the electrode surface via a histidine tag thereby enabling the redox mechanism of protein to be examined. When scanning the applied potential in the negative direction (cathodic), two one-electron reduction waves can be observed. The first of these redox waves occurs at −90 mV and is electrochemically reversible at all scan rates whereas the second wave occurs at −433 mV is irreversible. These two processes are interpreted as the initial reduction of the disulfide form of the protein to a stable (reversible) semi-reduced radical anion intermediate, followed by an electrochemically irreversible process to form a fully reduced thioredoxin. These electron transfer characteristics suggest that a radical intermediate retaining the sulfur-sulfur bond is thermodynamically stable but the addition of a second electron results in bond scission. |
Keywords: | direct electrochemistry disulfide protein gold electrode metal affinity protein immobilization radical intermediate thioredoxin |
Description: | The original publication can be found at www.springerlink.com |
DOI: | 10.1007/BF02442581 |
Published version: | http://dx.doi.org/10.1007/bf02442581 |
Appears in Collections: | Aurora harvest Molecular and Biomedical Science publications |
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