Special Issue "Sulfur Atom: Element for Adaptation to an Oxidative Environment 2016"
Deadline for manuscript submissions: closed (31 October 2016)
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 the oxygen concentration in the Earth’s atmosphere, sulfur atoms are 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.
Two years after the publication of the first Special Issue in 2014, a large number of investigations indicated large regulatory capacities of the endogenous pool of sulfide. Nowadays, the research in this area has focused on a variety of donor molecules used to investigate physiological action of sulfide in vitro.
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
- Sulfur Atom: Element for Adaptation to an Oxidative Environment in Molecules (12 articles)