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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 ...
BERNI R +3 more
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Ferredoxin activation by rhodanese
Phytochemistry, 1974Abstract Rhodanese was extracted from Brassica oleracea leaves and purified 150-fold. The enzyme was shown to have optimum activity at pH 8-8.5 and a temperature range of 50-55°; a Km of 0.4 mM at 30° for thiosulphate and cyanide. and mol. wt around 32000.
Umberto Tomati +2 more
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Soil Science Society of America Journal, 1976
Abstract The detection of rhodanese (enzyme catalyzes the formation of SCN ‐ from S 2 O 3 2‐ and CN ‐ ) in soils is reported, and a ...
M. A. Tabatabai, B. B. Singh
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Abstract The detection of rhodanese (enzyme catalyzes the formation of SCN ‐ from S 2 O 3 2‐ and CN ‐ ) in soils is reported, and a ...
M. A. Tabatabai, B. B. Singh
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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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Nano-intercalated rhodanese in cyanide antagonism
Nanotoxicology, 2010Present studies have focused on nano-intercalated rhodanese in combination with sulfur donors to prevent cyanide lethality in a prophylactic mice model for future development of an effective cyanide antidotal system. Our approach is based on the idea of converting cyanide to the less toxic thiocyanate before it reaches the target organs by utilizing ...
Ilona, Petrikovics +7 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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Selenium Binding to Beef‐Kidney Rhodanese
European Journal of Biochemistry, 1975The reaction of beef kidney rhodanese with selenosulfate was studied. The selenium‐treated enzyme shows an absorption spectrum with a maximum at 375 nm attributable to a sulfoselenide group. This absorption is bleached by addition of cyanide. After cyanide treatment stoichiometric amount of selenocyanate can be found.The intrinsic fluorescence of ...
C, Cannella +5 more
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Primary structure of avian hepatic rhodanese
Journal of Protein Chemistry, 1990Rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1.) was purified from chicken livers and its amino acid sequence was determined. The enzyme has a specific activity of 676 IU and a molecular weight of 32,255. The primary structure of 289 amino acids was solved by sequential Edman degradation of overlapping peptides obtained by selected ...
R A, Kohanski, R L, Heinrikson
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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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Rhodanese domain-containing sulfurtransferases
2019Sulfur is an essential element for the growth and development of plants, which synthesize cysteine and methionine from the reductive assimilation of sulfate. Besides its incorporation into proteins, cysteine is the building block for the biosynthesis of numerous sulfur-containing molecules and cofactors.
Selles, Benjamin +3 more
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