Rhodanese: an enzyme not necessary for thiosulphate oxidation byThiobacillusA2
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چکیده
منابع مشابه
Deficiency of thiosulphate sulphurtransferase (rhodanese) in Leber's hereditary optic neuropathy.
Leber's hereditary optic neuropathy is a rare cause of progressive visual failure. Its cause is unknown, but one hypothesis is that patients have a defect in the detoxication of cyanide. One of the enzymes used in this detoxication is thiosulphate sulphurtransferase (rhodanese). The activity of this enzyme was measured in the rectal mucosa of a group of subjects with Leber's hereditary optic ne...
متن کاملThiosulphate Oxidation in Thiobacillus
bacterium Thiobacillus X. A fifth fraction (acidic fraction) contained two additional cytochrome components with x bands at 550 and 557 msi respectively in the reduced state. 2. All the cytochromes appear to be ofthe c type, are labile to heat and acid and do not combine with carbon monoxide. They are auto-oxidizable to varying degrees. 3. Cytochromes 550 (1) and 557 (1) are basic, and are adso...
متن کاملThiosulphate Oxidation by Thiobacillus Strain C
1. Thiobacillus strain C oxidized [35S]thiosulphate completely to sulphate. 2. During thiosulphate oxidation [35S]sulphate was formed more rapidly from (S. 35SO3)2than from (35S *SO3)2-. 35S disappeared less rapidly from thiosulphate with (35S SO3)2as substrate than with (S.35SO3)2-. 3. Thiosulphate labelled in both atoms was produced during (35S * SO3)2oxidation, but not during (S. 35SO3)2oxid...
متن کاملMolecular cloning, sequencing and characterization of cDNA to rat liver rhodanese, a thiosulphate sulphurtransferase.
Rhodanese (EC 2.8.1.1), a mitochondrial thiosulphate sulphurtransferase, is involved in the formation of iron-sulphur complexes and cyanide detoxification. By screening a rat liver cDNA library with oligonucleotide probes complementary to portions of the published bovine rhodanese peptide sequence, rat rhodanese cDNA clones were obtained and sequenced. Comparison of the rat rhodanese cDNA open ...
متن کاملAn expanded mechanism for rhodanese catalysis.
The kinetic behavior of rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) was investigated at pH values from 5.0 to 10.8. The binding of thiosulfate was shown to be dependent upon a pK’ of 9.9, with the protonated enzyme binding the substrate much more strongly than the deprotonated form. An enzymic nucleophile displaces sulfite to form the sulfur-substituted enzyme. This reaction ...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1983
ISSN: 0378-1097,1574-6968
DOI: 10.1111/j.1574-6968.1983.tb00494.x