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Properties of Azotobacter vinelandii rhodanese.

Authors: S, Pagani; G, Sessa; F, Sessa; R, Colnaghi;

Properties of Azotobacter vinelandii rhodanese.

Abstract

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.

Related Organizations
Keywords

Molecular Weight, Azotobacter vinelandii, Kinetics, Cyanides, Thioctic Acid, Thiosulfates, Electrophoresis, Polyacrylamide Gel, Amino Acids, Chromatography, High Pressure Liquid, Thiosulfate Sulfurtransferase

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
18
Average
Top 10%
Average
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