Rhodanese is a sulfurtransferase which in vitro catalyzes the transfer of a sulfane sulfur from thiosulfate to cyanide. Ionic interactions of the prokaryotic rhodanese-like protein from Azotobacter vinelandii were studied by fluorescence and NMR spectroscopy. The catalytic Cys230 residue of the enzyme was selectively labelled using [15N]CyS, and changes in 1H and 15N NMR resonances on addition of different ions were monitored. The results clearly indicate that the sulfur transfer is due to a specific reaction of the persulfurated Cys residue with a sulfur acceptor such as cyanide and not to the presence of the anions. Moreover, the 1H-NMR spectrum of a defined spectral region is indicative of the status of the enzyme and can be used to directly monitor sulfur loading even at low concentrations. Selenium loading by the addition of selenodiglutathione was monitored by fluorescence and NMR spectroscopy. It was found to involve a specific interaction between the selenodiglutathione and the catalytic cysteine residue of the enzyme. These results indicate that rhodanese-like proteins may function in the delivery of reactive selenium in vivo.

Melino, S.m., Cicero, D.o., Orsale, M., Forlani, F., Pagani, S., Paci, M. (2003). Azotobacter vinelandii rhodanese Selenium loading and ion interaction studies, 270(20), 4208-4215 [10.1046/j.1432-1033.2003.03818.x].

Azotobacter vinelandii rhodanese Selenium loading and ion interaction studies

MELINO, SONIA MICHAELA;CICERO, DANIEL OSCAR;PACI, MAURIZIO
2003-01-01

Abstract

Rhodanese is a sulfurtransferase which in vitro catalyzes the transfer of a sulfane sulfur from thiosulfate to cyanide. Ionic interactions of the prokaryotic rhodanese-like protein from Azotobacter vinelandii were studied by fluorescence and NMR spectroscopy. The catalytic Cys230 residue of the enzyme was selectively labelled using [15N]CyS, and changes in 1H and 15N NMR resonances on addition of different ions were monitored. The results clearly indicate that the sulfur transfer is due to a specific reaction of the persulfurated Cys residue with a sulfur acceptor such as cyanide and not to the presence of the anions. Moreover, the 1H-NMR spectrum of a defined spectral region is indicative of the status of the enzyme and can be used to directly monitor sulfur loading even at low concentrations. Selenium loading by the addition of selenodiglutathione was monitored by fluorescence and NMR spectroscopy. It was found to involve a specific interaction between the selenodiglutathione and the catalytic cysteine residue of the enzyme. These results indicate that rhodanese-like proteins may function in the delivery of reactive selenium in vivo.
2003
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
N-15-NMR; Azotobacter vinelandii; rhodanese; selenodiglutathione; sulfurtransferase
Melino, S.m., Cicero, D.o., Orsale, M., Forlani, F., Pagani, S., Paci, M. (2003). Azotobacter vinelandii rhodanese Selenium loading and ion interaction studies, 270(20), 4208-4215 [10.1046/j.1432-1033.2003.03818.x].
Melino, Sm; Cicero, Do; Orsale, M; Forlani, F; Pagani, S; Paci, M
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/43615
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