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Chemical Modification of Rhodanese with Sulphite
Free Radical Research Communications, 1991The essential sulphydryl group of bovine liver rhodanese (thiosulphate: cyanide sulphurtrasferase, E.C. 2.8.1.1.) is modified by sulphite produced during the enzymatic reaction or added to the fully active enzyme. The enzyme treated with labelled reagent incorporates 1 equivalent of SO3(2-) and loses one -SH group with the formation of a S-sulphonate ...
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Is there rhodanese activity in plants?
Phytochemistry, 1992Abstract In view of the possible role of rhodanese in the HCN detoxification of cyanogenic plants, a method to measure low rhodanese levels is proposed. As the spontaneous formation of thiocyanate can mimic low levels of rhodanese activity, the influence of the composition of the reaction mixture on the spontaneous thiocyanate formation was studied ...
P Kakes
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Thermodynamics of zinc binding to rhodanese
Archives of Biochemistry and Biophysics, 1974Abstract The binding of zinc ion (Zn2+) to rhodanese at two pH values was studied by microcalorimetry and the free energy, enthalpy, and entropy changes determined. Binding exhibited rather large endothermic enthalpy changes quite similar to those observed for zinc-model compound interactions.
D W, Bolen, S, Rajender
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Active site peptides of rhodanese
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1970Abstract The active site cysteinyl peptide isolated from a tryptic digest of rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1) by column chromatography has been found to contain 15 amino acid residues, of which 7 are hydrophobic. The tryptophyl peptides in such digests also appear to consist predominantly of residues which are hydrophobic.
F, Detoma, J, Westley
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The double domain structure of rhodanese
Journal of Molecular Biology, 1975A 3 A electron density map of bovine liver rhodanese shows, in conjunction with gel electrophoresis experiments, that rhodanese consists of a single polypeptide chain with molecular weight of 32,000. The map reveals a very clear double domain structure of the molecule. The two domains are of equal size and have very similar conformations.
Bergsma, J. +5 more
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Phytochemistry, 1973
Abstract Rhodanese activity was detected in crude leaf extracts of 12 randomly selected plant species consisting of 9 non-cyanophoric and 3 cyanophoric species. In each case, the enzyme exhibited high activity at pH 10·4 and 55°. There appeared to be no correlation between rhodanese activity and the cyanophoric nature of the plant.
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Abstract Rhodanese activity was detected in crude leaf extracts of 12 randomly selected plant species consisting of 9 non-cyanophoric and 3 cyanophoric species. In each case, the enzyme exhibited high activity at pH 10·4 and 55°. There appeared to be no correlation between rhodanese activity and the cyanophoric nature of the plant.
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Phytochemistry, 1972
Abstract Rhodanese activity was detected in a crude extract of tapioca ( Manihot utilissima ) leaves. Optimal activity was found at a high pH (10·2–11·0) and temperature (57–59°). Under these conditions, rhodanese from 0·5 ml of the crude extract (75 mg leaf fr. wt.) catalysed the formation of 10·2 μmoles thiocyanate per 15 min.
M.Y. Chew, C.G. Boey
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Abstract Rhodanese activity was detected in a crude extract of tapioca ( Manihot utilissima ) leaves. Optimal activity was found at a high pH (10·2–11·0) and temperature (57–59°). Under these conditions, rhodanese from 0·5 ml of the crude extract (75 mg leaf fr. wt.) catalysed the formation of 10·2 μmoles thiocyanate per 15 min.
M.Y. Chew, C.G. Boey
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Determination of rhodanese in plants
Phytochemistry, 1990Abstract The standard rhodanese test used for extracts from animal tissues does not work in plant homogenates due to the concomitant occurrence of both enzymatic and non-enzymatic thiocyanate production. Rhodanese activity is generally determined by the enzymatic formation of SCN − from thiosulphate and cyanide.
Reinhard Lieberei, Dirk Selmar
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Occurrence of Rhodanese in a Species of Thiobacillus
Nature, 1958THE enzyme rhodanese which catalyses the reaction: has been shown to be present in Thiobacillus thiocyanoxidans. Cells of the organism, grown in thiosulphate medium with forced aeration and 2–5 per cent of carbon dioxide added1, were harvested in a de Laval centrifugal separator ...
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Cyanide detoxification by recombinant bacterial rhodanese
Chemosphere, 2006Cyanide is a major environmental pollutant of the chemical and metallurgical industries. Although extremely toxic, cyanide can enzymatically be converted to the less toxic thiocyanate by rhodaneses (thiosulfate:cyanide sulfurtransferases, EC 2.8.1.1). We engineered a genetic system to express high levels of recombinant Pseudomonas aeruginosa rhodanese (
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