期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1794, 期 8, 页码 1218-1223出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2009.04.001
关键词
Thioredoxin system; Yeast; Glutathione; Kinetic parameters; Reduction efficiency
资金
- Ministry of Science and Technology of China [2006CB910202, 2006CB806501]
- National Natural Science Foundation of China [30670461, 30870490]
- Ministry of Education of China [NCET-06-0374, PRA B07-02]
Thioredoxin (Trx) and glutathione/glutaredoxin (GSH/Grx) systems play the dominant role in cellular redox homeostasis. Recently the Trx system has been shown to be responsible to control the balance of GSH/GSSG once the glutathione reductase system is not available. To decipher the structural basis of electron transfer from the Trx system to GSSG, we solved the crystal structures of oxidized Trx1 and glutathionylated Trx1Cys33Ser mutant at 1.76 and 1.80 angstrom, respectively. Comparative structural analysis revealed a key residue Met35 involved in the Trx-GSSC recognition. Subsequent mutagenesis and kinetic studies proved that Met35Arg mutation could alter the apparent K-m and V-max values of the reaction. These findings gave us the structural insights into GSSG reduction catalyzed by the Trx system. (C) 2009 Elsevier B.V. All rights reserved.
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