Special Issue "Sulfur Atom: Element for Adaptation to an Oxidative Environment"
Deadline for manuscript submissions: closed (31 October 2014)
Dr. Noriyuki Nagahara
Isotope Research Center, Nippon Medical School, 1-1-5 Sendagi, Bunkyo-ku, Tokyo 113-8602, Japan
Interests: stress; oxygen atoms; oxidation and reduction; persulfide; protein function; redox chemistry; sulfane sulfur atoms; sulfur atoms; sulfur compounds; sulfurtransferase
During the rise of oxygen concentration in the earth’s atmosphere, a sulfur atom is incorporated into proteins as the redox-active cysteine residue, and antioxidant molecules, such as thioredoxin, glutathione, and glutaredoxin appear. Cysteine residues in proteins first form intra- and inter-molecular disulfides to maintain protein (peptide) structure and also to regulate protein function. Secondly, the redox-active cysteine residues are known to regulate proteins redox state and function by reversible oxidation to cysteinosulfenic or cysteinosulfinic residues or by -SH group sulfuration to persulfides. Finally, cysteine residues of catalytic sites of such enzymes as sulfurtransferases and sulfotransferases, contributing to the transfer of elemental sulfur and sulfenate, respectively, are involved in sulfur metabolism. Recently, sulfur atoms, at reduced oxidation state, of hydrogen sulfide and polysulfides have been recognized as important molecules in the regulation of many physiological processes. The Editors’ intent is to collect both review and original papers on the above subjects in a special issue.
Dr. Noriyuki Nagahara
Dr. Maria Wrobel
Manuscript Submission Information
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- cysteine metabolism
- hydrogen sulfide
- oxidative stress
- oxygen atoms; oxidation
- protein function
- redox chemistry
- sulfane sulfur atoms
- sulfur atoms
- sulfur compounds