Direct Electrochemical Characterization of Archaeal Thioredoxins

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....

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Bibliographic Details
Published in:Angewandte Chemie (International ed.) 2007-01, Vol.46 (22), p.4145-4147
Main Authors: Chobot, Sarah E., Hernandez, Hector H., Drennan, Catherine L., Elliott, Sean J.
Format: Article
Language:English
Subjects:
Archaea - chemistry
Archaeal Proteins - analysis
Archaeal Proteins - metabolism
disulfide bonds
Disulfides
Electrochemistry
electron transfer
Electron Transport
Hydrogen-Ion Concentration
Models, Molecular
Oxidation-Reduction
proteins
redox chemistry
Temperature
Thioredoxins - analysis
Thioredoxins - metabolism
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Summary: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.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200604620