Display Settings:

Format

Send to:

Choose Destination
    Antioxid Redox Signal. 2008 Sep;10(9):1549-64.

    Thiol chemistry in peroxidase catalysis and redox signaling.

    Source

    Institute of Neurosciences (CNR) c/o Department of Biological Chemistry, University of Padova (Italy). alberto.bindoli@bio.unipd.it

    Abstract

    The oxidation chemistry of thiols and disulfides of biologic relevance is described. The review focuses on the interaction and kinetics of hydrogen peroxide with low-molecular-weight thiols and protein thiols and, in particular, on sulfenic acid groups, which are recognized as key intermediates in several thiol oxidation processes. In particular, sulfenic and selenenic acids are formed during the catalytic cycle of peroxiredoxins and glutathione peroxidases, respectively. In turn, these enzymes are in close redox communication with the thioredoxin and glutathione systems, which are the major controllers of the thiol redox state. Oxidants formed in the cell originate from several different sources, but the major producers are NADPH oxidases and mitochondria. However, a different role of the oxygen species produced by these sources is apparent as oxidants derived from NADPH oxidase are involved mainly in signaling processes, whereas those produced by mitochondria induce cell death in pathways including also the thioredoxin system, presently considered an important target for cancer chemotherapy.

    PMID:
    18479206
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC2693905
    Free PMC Article

    Images from this publication.See all images (4) Free text

    FIG. 2.
    FIG. 4.
    FIG. 1.
    FIG. 3.

      Supplemental Content

      Icon for Mary Ann Liebert, Inc. Icon for PubMed Central

      Save items

      loading

      Recent activity

      Your browsing activity is empty.

      Activity recording is turned off.

      Turn recording back on

      See more...
      Write to the Help Desk