Three classes of methionine sulfoxide reductases are known: MsrA and MsrB which are
implicated stereo-selectively in the repair of protein oxidized on their methionine residues; …

Thiol redox chemical reactions play a key role in a variety of physiological processes, mainly
due to the presence of low-molecular-weight thiols and cysteine residues in proteins …

Methionine sulfoxide reductase A (MsrA) enzymes have recently found applications as
nonoxidative biocatalysts in the enantioselective kinetic resolution of racemic sulfoxides …

The oxidation of Met to methionine sulfoxide (MetSO) by oxidants such as hydrogen
peroxide, hypochlorite, or peroxynitrite has profound effects on protein function. This …

Sulfoxides and selenoxides oxidize thiols to disulfides while being reduced back to sulfides
and selenides. While the reduction mechanism of sulfoxides to sulfides has been thoroughly …

Neisseria meningitidis, an obligate pathogenic bacterium in humans, has acquired different
defense mechanisms to detect and fight the oxidative stress generated by the host's defense …

Protein tyrosine phosphatase 1B (PTP1B) is a key enzyme in a variety of physiological
processes including insulin and leptin signaling. Experimentally it has been previously …

Elucidating the origin of enzymatic catalysis stands as one the great challenges of
contemporary biochemistry and biophysics. The recent emergence of computational …

Methionine sulfoxide reductase A (MsrA) reduces free and protein-based methionine-S-
sulfoxide to methionine. Structures of 1-Cys MsrAs lacking a resolving Cys, which interacts …

The mouse methionine sulfoxide reductase A (MsrA) belongs to the subclass of MsrAs with
one catalytic and two recycling Cys corresponding to Cys51, Cys198 and Cys206 in …