Hydrogen peroxide (H2O2) is continuously formed by the autoxidation of redox enzymes in
aerobic cells, and it also enters from the environment, where it can be generated both by …

Peroxiredoxins (Prxs), some of nature's dominant peroxidases, use a conserved Cys residue
to reduce peroxides. They are highly expressed in organisms from all kingdoms, and in …

Thiol peroxidases comprise glutathione peroxidases (GPx) and peroxiredoxins (Prx). The
enzymes of both families reduce hydroperoxides with thiols by enzyme-substitution …

Peroxiredoxins (Prdxs) sense and assess peroxide levels, and signal through protein
interactions. Understanding the role of the multiple structural and post-translational …

Protein–protein associations, ie formation of permanent or transient protein complexes, are
essential for protein functionality and regulation within the cellular context. Peroxiredoxins …

Thiol-disulfide interconversions play a crucial role in the chemistry of biological systems.
They participate in the major systems that control the cellular redox potential and prevent …

Thiol peroxidases are ubiquitous recently characterized heme-free peroxidases, which
catalyze the reduction of peroxynitrites and of various peroxides by catalytic cysteine …

The thioredoxin fold is found in proteins that serve a wide variety of functions. Among these
are peroxiredoxins, which catalyze the reduction of hydrogen peroxide and alkyl peroxides …

Local levels of active thyroid hormone (3, 3′, 5-triiodothyronine) are controlled by the action
of activating and inactivating iodothyronine deiodinase enzymes. Deiodinases are …

The high resolution 2‐D protein gel electrophoresis technique combined with MALDI‐TOF
MS and a recently developed fluorescence‐based thiol modification assay were used to …