
Rhodanese (thiosulfate: cyanide sulfurtransferase, E.C. 2.8.1.1) was purified from the nitrogen fixing organism Azotobacter vinelandii, and its amino acid composition was determined. The enzyme is a single polypeptide chain of M(r) 29,000 which showed an apparent pI of 4.7 and no presence of isoenzymes. Steady-state initial velocity measurements indicate that the enzyme catalyzes the transfer of sulfane sulfur of thiosulfate either to cyanide or to dihydrolipoate by way of a double displacement mechanism.
Molecular Weight, Azotobacter vinelandii, Kinetics, Cyanides, Thioctic Acid, Thiosulfates, Electrophoresis, Polyacrylamide Gel, Amino Acids, Chromatography, High Pressure Liquid, Thiosulfate Sulfurtransferase
Molecular Weight, Azotobacter vinelandii, Kinetics, Cyanides, Thioctic Acid, Thiosulfates, Electrophoresis, Polyacrylamide Gel, Amino Acids, Chromatography, High Pressure Liquid, Thiosulfate Sulfurtransferase
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