Cysteine is one of the least abundant amino acids, yet it is frequently found as a highly
conserved residue within functional (regulatory, catalytic, or binding) sites in proteins. It is …

Reactive oxygen, nitrogen, and sulfur species, referred to as ROS, RNS, and RSS,
respectively, are produced during normal cell function and in response to various stimuli. An …

Hydrogen peroxide (H2O2) is a well-documented component of living cells. It plays
important roles in host defense and oxidative biosynthetic reactions. In addition there is …

The Escherichia coli transcription factor OxyR is activated by the formation of an
intramolecular disulfide bond and subsequently is deactivated by enzymatic reduction of the …

Riboflavin (RF) and its active forms, the cofactors flavin mononucleotide (FMN) and flavin
adenine dinucleotide (FAD), have been extensively used in the food, feed and …

Reactive (low pKa) cysteine residues in proteins are critical components in redox signaling.
A particularly reactive and versatile reversibly oxidized form of cysteine, the sulfenic acid …

While it has been known for more than 20 years that unusually stable cysteine-sulfenic acid
(Cys-SOH) derivatives can be introduced in selected proteins by mild oxidation, only …

The flavoprotein disulfide reductases represent a family of enzymes that show high
sequence and structural homology. They catalyze the pyridine-nucleotide-dependent …

Despite much recent interest in the biochemistry of reactive oxygen species, the
mechanisms by which hydrogen peroxide (H2O2) functions in mammalian cells remain …

Oxidative cysteine modifications have emerged as a central mechanism for dynamic post-
translational regulation of all major protein classes and correlate with many disease states …