The high resolution three-dimensional structure of bovine liver rhodanese.

[1]  W. Hol,et al.  Binding of metal cyanide complexes to bovine liver rhodanese in the crystalline state. , 1983, Biochemistry.

[2]  K. Rhyner,et al.  THIOSULPHATE-SULPHUR TRANSFERASE (RHODANESE) DEFICIENCY IN LEBER'S HEREDITARY OPTIC ATROPHY , 1981, The Lancet.

[3]  W. Fitch,et al.  An examination of the expected degree of sequence similarity that might arise in proteins that have converged to similar conformational states. The impact of such expectations on the search for homology between the structurally similar domains of rhodanese. , 1981, Journal of molecular biology.

[4]  H. Felbeck.  Chemoautotrophic Potential of the Hydrothermal Vent Tube Worm, Riftia pachyptila Jones (Vestimentifera). , 1981, Science.

[5]  J. Westley.  Chapter 13 – Rhodanese and the Sulfane Pool , 1980 .

[6]  A. Koj,et al.  Subcellular compartmentation of rhodanese and 3-mercaptopyruvate sulphurtransferase in the liver of some vertebrate species , 1980 .

[7]  William B. Jakoby,et al.  Enzymatic basis of detoxication , 1980 .

[8]  W. Hol,et al.  The structure of bovine liver rhodanese. II. The active site in the sulfur-substituted and the sulfur-free enzyme. , 1979, Journal of molecular biology.

[9]  R. Heinrikson,et al.  The covalent structure of bovine liver rhodanese. Isolation and partial structural analysis of cyanogen bromide fragements and the complete sequence of the enzyme. , 1978, The Journal of biological chemistry.

[10]  M. Volini,et al.  Effects of metal-ion binding on rhodanese activity. , 1978, Archives of biochemistry and biophysics.

[11]  W. Hol,et al.  Structure of bovine liver rhodanese. I. Structure determination at 2.5 A resolution and a comparison of the conformation and sequence of its two domains. , 1978, Journal of molecular biology.

[12]  W. Hol,et al.  The covalent and tertiary structure of bovine liver rhodanese , 1978, Nature.

[13]  S. Pagani,et al.  Insertion of sulfide into ferredoxins catalyzed by rhodanese , 1977, FEBS letters.

[14]  S. Pagani,et al.  Rhodanese-Mediated sulfur transfer to succinate dehydrogenase. , 1977, European journal of biochemistry.

[15]  W G Hol,et al.  The double domain structure of rhodanese. , 1975, Journal of molecular biology.

[16]  S. Oi.  Inhibition of rat liver rhodanese by di-, tricarboxylic, and alpha-keto acids. , 1975, Journal of Biochemistry (Tokyo).

[17]  B. Sörbo.  CHAPTER 10 – Thiosulfate Sulfurtransferase and Mercaptopyruvate Sulfurtransferase , 1975 .

[18]  J. Drenth,et al.  STRUCTURE OF RHODANESE AT 4A RESOLUTION CONFORMATION OF POLYPEPTIDE-CHAIN , 1974 .

[19]  S. F. Wang,et al.  The interdependence of substrate and protein transformations in rhodanese catalysis. I. Enzyme interactions with substrate, product, and inhibitor anions. , 1973, The Journal of biological chemistry.

[20]  G. Federici,et al.  Effect of Sulfur Binding on Rhodanese Fluorescence , 1972 .

[21]  P. Horowitz,et al.  Improved preparation of bovine liver rhodanese. , 1970, The Journal of biological chemistry.

[22]  J. Westley,et al.  The mechanism of the rhodanese-catalyzed thiosulfate-cyanide reaction. Thermodynamic and activation parameters. , 1968, The Journal of biological chemistry.

[23]  J. Wilson.  Leber's hereditary optic atrophy: a possible defect of cyanide metabolism. , 1965, Clinical science.

[24]  J. Westley,et al.  Mechanism of rhodanese action: isotopic tracer studies. , 1962, The Journal of biological chemistry.

[25]  D. Reinwein.  Die Verteilung der Thiosulfat-Schwefeltransferase und des Rhodanids im menschlichen und tierischen Organismus , 1961 .

[26]  R. Wattiaux,et al.  Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue. , 1955, The Biochemical journal.