Rhodanese is a mitochondrial enzyme that detoxifies cyanide (CN−) by converting it to thiocyanate (SCN−, also known as "rhodanate").[1] In enzymatology, the common name is listed as thiosulfate sulfurtransferase (EC 2.8.1.1).[2] The diagram on the right shows the crystallographically-determined structure of rhodanese.
It catalyzes the following reaction:
thiosulfate + cyanide sulfite + thiocyanate
^Cipollone R, Ascenzi P, Tomao P, Imperi F, Visca P (2008). "Enzymatic detoxification of cyanide: clues from Pseudomonas aeruginosa Rhodanese". Journal of Molecular Microbiology and Biotechnology. 15 (2–3): 199–211. doi:10.1159/000121331. PMID 18685272. S2CID 25431686.
^EC 2.8.1.1, at the International Union of Biochemistry and Molecular Biology
Rhodanese is a mitochondrial enzyme that detoxifies cyanide (CN−) by converting it to thiocyanate (SCN−, also known as "rhodanate"). In enzymatology,...
Malekhusseini A, Akrami F, Ebrahimnejad H (2006). "Cyanide-metabolizing enzyme rhodanese in human tissues: Comparison with domestic animals". Comparative Clinical...
exception is cyanide, which can be metabolized by the liver. The enzyme rhodanese converts the cyanide into the much less toxic thiocyanate. This process...
is by enzymatic conversion to thiocyanate by the mitochondrial enzyme rhodanese. Thiocyanate is a relatively non-toxic molecule and is excreted by the...
is however still used for the treatment of a hypertensive emergency. Rhodanese catalyzes the reaction of sodium nitroprusside (like other cyanides) with...
contained low concentrations of beta-glucosidases and high concentrations of rhodanese, which converts HCN to the less toxic thiocyanate. Later, however, it...
small quantities. It is metabolized by rhodanese, a live enzyme at a rate of approximately 17 μg/kg·min. Rhodanese catalyzes the irreversible reaction forming...
cyanide produced to be detoxified within the body to thiocyanate (the rhodanese pathway). It also allows more of the acetonitrile to be excreted unchanged...
(eight per ring). It has been shown to fold the mitochondrial protein rhodanese; however, no natural substrates have yet been identified. Group II chaperonins...
reaction with a sulfur-donor such as thiosulfate, catalysed by the enzyme rhodanese. In the absence of sufficient thiosulfate, cyanide ions can quickly reach...
cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry". Biochemistry. 44 (21): 7912–20...
cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry". Biochemistry. 44 (21): 7912–20...
presumed to be bicarbonate uptake permeases. Another has SulP fused to Rhodanese, a sulfate:cyanide sulfotransferase (TC# 2.A.53.9.1). This SulP homologue...
"Enzymatic detoxification of cyanide: clues from Pseudomonas aeruginosa Rhodanese". Journal of Molecular Microbiology and Biotechnology. 15 (2–3): 199–211...
(1993). "Limited tryptic digestion near the amino terminus of bovine liver rhodanese produces active electrophoretic variants with altered refolding". J. Biol...
EM, Dhe-Paganon S (December 2006). "Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific...
concentrations in the trophosome, but are absent in the muscle. Furthermore, rhodanese, APSreductase, and ATP-sulfurylase are involved in adenosine triphosphate...
"Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese". Eur. J. Biochem. 231 (2): 312–316. doi:10.1111/j.1432-1033.1995.tb20702...
catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain". J. Mol. Biol. 282 (1): 195–208. doi:10.1006/jmbi.1998...
Newman EM, Dhe-Paganon S (2006). "Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific...
Leimkühler S (April 2004). "Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans"...
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