Thioredoxin (Trx) and thioredoxin reductase (TrxR) are essential components of the Trx
system which plays pivotal roles in regulating multiple cellular redox signaling pathways. In …

Proteins are a major target for oxidants as a result of their abundance in biological systems,
and their high rate constants for reaction. Kinetic data for a number of radicals and non …

Thioredoxin is known as a hydrogen donor for ribonucleotide reductase, the essential
enzyme providing deoxyribonucleotides for DNA replication (1-4). Characterization of viable …

Methionine (Met) is one of the most readily oxidized amino acid constituents of proteins. It is
attacked by H2O2, hydroxyl radicals, hypochlorite, chloramines, and peroxynitrite, all these …

Thioredoxin and glutaredoxin systems in mammalian cells utilize thiol and selenol groups to
maintain a reducing intracellular redox state acting as antioxidants and reducing agents in …

Biochemistry of the Amino Acids, Second Edition, Volume II focuses on the trends in
research on amino acids and biochemistry. Given considerations are incorporation of amino …

The crystal structure of thioredoxin from Escherichia coli has been refined by the
stereochemically restrained least-squares procedure to a crystallographic R-factor of 0.165 …

An enzyme that catalyzes the reduction of methionine sulfoxide residues in ribosomal
protein L12 has been partially purified from Escherichia coli extracts. Methionine sulfoxide …

Reactive oxygen and nitrogen intermediates can cause damage to many cellular
components and have been implicated in a number of diseases. Cells have developed a …

An enzyme that can reduce methionine sulfoxide in proteins was first discovered in
Escherichia coli about 25 years ago. It is now apparent that there is a family of enzymes …