AI Article Synopsis
- A novel method combines front-face fluorescence spectroscopy with a transparent electrochemical cell to study protein electrochemical properties.
- The study focused on the redox changes in tryptophans within cytochrome c, achieving successful redox potential measurements.
- Additionally, the fluorescence analysis of thiol-disulfide oxidoreductases SoxS and SoxW revealed distinct midpoint potentials, with SoxS being crucial for sulfur oxidation in a specific bacterium, while SoxW is not essential.
Article Abstract
A new way to study the electrochemical properties of proteins by coupling front-face fluorescence spectroscopy with an optically transparent thin-layer electrochemical cell is presented. First, the approach was examined on the basis of the redox-dependent conformational changes in tryptophans in cytochrome c, and its redox potential was successfully determined. Second, an electrochemically induced fluorescence analysis of periplasmic thiol-disulfide oxidoreductases SoxS and SoxW was performed. SoxS is essential for maintaining chemotrophic sulfur oxidation of Paracoccus pantotrophus active in vivo, while SoxW is not essential. According to the potentiometric redox titration of tryptophan fluorescence, the midpoint potential of SoxS was -342 ± 8 mV versus the standard hydrogen electrode (SHE') and that of SoxW was -256 ± 10 mV versus the SHE'. The fluorescence properties of the thioredoxins are presented and discussed together with the intrinsic fluorescence contribution of the tyrosines.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1021/bi1013112 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!