Selenium binding to beef-kidney rhodanese.
The reaction of beef kidney rhodanese with selenosulfate was studied. The selenium-treated enzyme shows an absorption spectrum with a maximum at 375 nm attributable to a sulfoselenide group. This absorption is bleached by addition of cyanide. After cyanide treatment stoichiometric amount of selenocyanate can be found. The intrinsic fluorescence of rhodanese is quenched by addition of stoichiometric selenosulfate. This effect can be reversed by cyanide or sulfite but not by selenite or glutathione. By comparison with model complexes the selenium-rhodanese intermediate was identified as a cysteinyl-selenium derivative.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002855:Chromatography, Thin Layer; D003485:Cyanates; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D011485:Protein Binding; D012643:Selenium; D018036:Selenium Compounds; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013431:Sulfates; D013466:Sulfurtransferases; D013884:Thiosulfate Sulfurtransferase
D003485:Cyanates; D018036:Selenium Compounds; D013431:Sulfates; D013466:Sulfurtransferases; D013884:Thiosulfate Sulfurtransferase; D012643:Selenium; C519925:sodium selenosulfate