Redox properties of the A-domain of the HMGB1 protein.
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ABSTRACT:
SUBMITTER: Sahu D
PROVIDER: S-EPMC2614879 | biostudies-literature | 2008 Dec
REPOSITORIES: biostudies-literature
Publications
Redox properties of the A-domain of the HMGB1 protein.
Sahu Debashish D Debnath Priyanka P Takayama Yuki Y Iwahara Junji J
FEBS letters 20081106 29
The High Mobility Group B1 (HMGB1) protein plays important roles in both intracellular (reductive) and extracellular (oxidative) environments. We have carried out quantitative investigations of the redox chemistry involving Cys22 and Cys44 of the HMGB1 A-domain, which form an intramolecular disulfide bond. Using NMR spectroscopy, we analyzed the real-time kinetics of the redox reactions for the A-domain in glutathione and thioredoxin systems, and also determined the standard redox potential. The ...[more]
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