Domain structural flexibility in rhodanese examined by quenching of a phosphorescent probe
- 1 November 1987
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 916 (2) , 236-244
- https://doi.org/10.1016/0167-4838(87)90114-2
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Active site modifications quench intrinsic fluorescence of rhodanese by different mechanismsBiochemistry, 1986
- The high resolution three-dimensional structure of bovine liver rhodaneseFundamental and Applied Toxicology, 1983
- Penetration of small molecules into proteins studied by quenching of phosphorescence and fluorescenceBiochemistry, 1983
- Penetration of dioxygen into proteins studied by quenching of phosphorescence and fluorescenceBiochemistry, 1983
- A nuclear magnetic relaxation study of conformational changes induced by substrate and temperature in bovine liver thiosulfate sulfurtransferase and yeast hexokinaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- A Fluorescence study of conformational changes induced by substrate and temperature in bovine liver thiosulfate sulfurtransferaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- The covalent and tertiary structure of bovine liver rhodaneseNature, 1978
- The Interdependence of Substrate and Protein Transformations in Rhodanese CatalysisJournal of Biological Chemistry, 1973
- The Mechanism of the Rhodanese-catalyzed Thiosulfate-Cyanide ReactionPublished by Elsevier ,1968
- Crystalline Rhodanese. I. Purification and Physicochemical Examination.Acta Chemica Scandinavica, 1953