disulfide bond

(redirected from Persulfide)
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disulfide bond

[dī¦səl‚fīd ′bänd]
(organic chemistry)
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
References in periodicals archive ?
Novel signaling molecules linked to polysulfide ([H.sub.2][S.sub.n]) such as hydrogen persulfide and trisulfide ([H.sub.2][S.sub.2] and [H.sub.2][S.sub.3]) help maintain neuronal transmission, vascular tone, cytoprotection, inflammation, and oxygen-sensing.
The first enzyme is sulfide:quinone oxidoreductase, which is located in the MIM where it oxidizes sulfide ([H.sub.2]S) to persulfide (R-SSH) and transfers two electrons to the ubiquinone pool, as described by Theissen and Martin (2008).
The persulfide group was removed from substrate cysteine and transferred to Cys356.
The mitochondrial dioxygenase gene ETHE1 encodes a mitochondrial enzyme involved in sulfide detoxification, which uses molecular [O.sub.2] and water to oxidize the mobile persulfide from quinone oxidoreductase to form sulfite, which in turn is involved in sulfur metabolism and takes part in the pathway in which [H.sub.2]S is oxidized to thiosulfate in three steps [57].
Bound sulfane sulfur is incorporated into proteins as persulfide or polysulfide, which release [H.sub.2]S under reducing conditions (see Fig.
Thioredoxin-dependent Peroxidase activity, peroxiredoxin peroxide reductase activity Glutathione S-transferase Conjugation of reduced glutathione to a P wide number of exogenous and endogenous substrates Persulfide dioxygenase Plays ab essential role in hydrogen ETHE1, mitochondrial sulfide catabolism in the mitochondrial matrix Protein folding/stress Tubulin-specific Involves the early step of the tubulin chaperone A folding pathway.
The observed antioxidative effects of [H.sub.2]S treatment in our setting may in part be explained by the potential of the gas to scavenge free radicals [7], or by upregulation of glutathione persulfide production in mitochondria [37].
In a similar manner, S-sulfhydration is a posttranslational modification of specific residues, through the formation of persulfide (-SSH) bonds.
[H.sub.2]S can store its sulfur group with iron (acid labile sulfur) [15] or in sulfane sulfur (a persulfide) [16] in mammalian tissues.
In the presence of oxygen, sulfide:quinone oxidoreductases (SQR) oxidize [H.sub.2]S to persulfide which is subsequently oxidized into sulfite via dioxygenase.
They suggested that gasotransmitter regulation of gametogenesis may occur through cysteine residue modification of target proteins, including formation of nitrosothiols and persulfides. Further studies of gasotransmitters on gametogenesis are necessary to further establish the potential for advancement of human assisted reproductive technology and reproduction therapy.