Results 161 to 170 of about 3,363 (208)
Structure, 2001 Background: Rhodanese domains are structural modules occurring in the three major evolutionary phyla. They are found as single-domain proteins, as tandemly repeated modules in which the C-terminal domain only bears the properly structured active site, or
Andrea Spallarossa +2 more
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FEBS Letters, 2000 The existence of rhodanese (thiosulfate:cyanide sulfurtransferase; EC 2.8.1.1) in plants has been highly controversial. We have isolated and characterized for the first time in plants two cDNAs encoding rhodanese isoforms in Arabidopsis thaliana, AtRDH1 ...
Kazuki Saito
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Journal of Chemical Ecology, 1985
Forty-four species of insects were assayed for the presence of rhodanese, an enzyme generally considered to be responsible for the detoxification of cyanide. Rhodanese was found to be widely distributed in both adults and larvae and was not restricted to those species which encounter exogenous cyanide through feeding on cyanogenic plants. These results
Stephen G Compton +2 more
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Forty-four species of insects were assayed for the presence of rhodanese, an enzyme generally considered to be responsible for the detoxification of cyanide. Rhodanese was found to be widely distributed in both adults and larvae and was not restricted to those species which encounter exogenous cyanide through feeding on cyanogenic plants. These results
Stephen G Compton +2 more
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Immunohistochemical localization of rhodanese
The Histochemical Journal, 1990The role of rhodanese in the detoxication of acute cyanide exposure is controversial. The debate involves questions of the availability of rhodanese to cyanide in the peripheral circulation. Blood-borne cyanide will distribute to the brain and may induce lesions or even death.
M, Sylvester, C, Sander
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Reaction of rhodanese with dithiothreitol
Biochimica et Biophysica Acta (BBA) - Enzymology, 1976The reaction between bovine rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1) and reduced dithiothreitol has been studied. This reagent, in the absence of thiosulfate, reduces the amount of sulfur carried by rhodanese with formation of sulfide and oxidized dithiothreitol: E-S-SH + reduced dithiothreitol replaced by E-SH + HS- + oxidized ...
L, Pecci +4 more
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Recombinant bovine rhodanese: purification and comparison with bovine liver rhodanese
BBA - Proteins and Proteomics, 1992Recombinant bovine rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) has been purified to homogeneity from Escherichia coli BL21(DE3) by cation-exchange chromatography. Recombinant and bovine liver rhodanese coelectrophorese under denaturing conditions, with an apparent subunit molecular weight of 33,000.
David M Miller +2 more
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Rhodanese as a thioredoxin oxidase
The International Journal of Biochemistry & Cell Biology, 2000A major catalytic difference between the two most common isoforms of bovine liver mitochondrial rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) has been observed. Both isoforms were shown to be capable of using reduced thioredoxin as a sulfur-acceptor substrate.
D L, Nandi, P M, Horowitz, J, Westley
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Biochemical and Biophysical Research Communications, 1971
Abstract The binding of zinc ion to bovine beef liver rhodanese has been investigated by nuclear magnetic resonance and emission spectroscopic methods. One equivalent of zinc ion is found to bind strongly to the enzyme; however, zinc is absent in the fully active native enzyme and the addition of zinc ion does not enhance catalytic activity.
R G, Bryant, S, Rajender
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Abstract The binding of zinc ion to bovine beef liver rhodanese has been investigated by nuclear magnetic resonance and emission spectroscopic methods. One equivalent of zinc ion is found to bind strongly to the enzyme; however, zinc is absent in the fully active native enzyme and the addition of zinc ion does not enhance catalytic activity.
R G, Bryant, S, Rajender
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The cystathionase-rhodanese system
Biochimica et Biophysica Acta (BBA) - Enzymology, 1967Abstract Cystathionase ( l -homoserine hydrolase (deaminating), EC 4.2.1.15) and rhodanese ∗∗ (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) have been combined to form a coupled enzyme system which is capable of utilizing cysteine sulfur for transsulfuration. The initial product of the action of Cystathionase on cystine, thiocysteine, is, at
T W, Szczepkowski, J L, Wood
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