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World J Biol Chem. Feb 26, 2014; 5(1): 68-74
Published online Feb 26, 2014. doi: 10.4331/wjbc.v5.i1.68
Published online Feb 26, 2014. doi: 10.4331/wjbc.v5.i1.68
Thioredoxin and glutaredoxin-mediated redox regulation of ribonucleotide reductase
Rajib Sengupta, Arne Holmgren, Division of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institute, SE-17177 Stockholm, Sweden
Author contributions: Sengupta R and Holmgren A contributed equally to this work, generated the figures and wrote the manuscript.
Supported by The Swedish Research Council Medicine, No. 3529; The Swedish Cancer Society, No. 961; The Wallenberg Foundation
Correspondence to: Rajib Sengupta, PhD, Division of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institute, Scheeles Vag 2, SE-17177 Stockholm, Sweden. rajib.sengupta@ki.se
Telephone: +46-8-52487727 Fax: +46-8-7284716
Received: November 7, 2013
Revised: December 17, 2013
Accepted: January 13, 2014
Published online: February 26, 2014
Revised: December 17, 2013
Accepted: January 13, 2014
Published online: February 26, 2014
Core Tip
Core tip: Thioredoxin and glutaredoxin-mediated redox regulations of ribonucleotide reductase (RNR) catalysis play a vital role as the RNR catalysis involves different redox active thiol functions, thiyl radicals and thiol proteins. The in depth knowledge of the whole redox catalysis will contribute significantly to designing and developing new RNR inhibitors for improved cancer chemotherapy, antibiotic development and antiviral treatments.