Publication | Closed Access
Direct Electrochemical Characterization of Archaeal Thioredoxins
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Citations
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References
2007
Year
Protein Quality ControlArchaeal ThioredoxinsProtein SecretionBiochemistryReversible 2Natural SciencesBioelectrochemistryBioelectrochemical SystemMolecular BiologyMicrobiologyAnalytical UltracentrifugationCellular BiochemistryRedox-active Disulfide BondMedicineProtein TransportRedox BiologyElectrochemistryDifferent Trx Proteins
Send and deliver: The thioredoxin (Trx) superfamily of proteins contains small soluble proteins that function as 2 e−/2 H+ electron-transfer agents by virtue of a redox-active disulfide bond. A fully reversible 2 e− disulfide-bond redox couple can be observed for four different Trx proteins. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2007/z604620_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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