Unfolding and inactivation of monomeric superoxide dismutase from E. coli by SDS.
The inactivation and the unfolding of the naturally monomeric Cu, Zn, superoxide dismutase from E. coli upon addition of sodium dodecylsulphate have been studied. In contrast to the bovine enzyme, CD, EPR, NMR spectroscopy and pulsed low resolution NMR measurements found an unfolding transition followed by inactivation of the enzyme. During this transition the active site becomes accessible to the bulk water. The unfolding is reversible and both, the tridimensional structure of the protein and the active site, can be restored upon dialysis. In addition, unfolding occurs without loss of metals in the solution.
Bozzi
M
M
Department of Chemical Science and Technology, Tor Vergata University, Via della Ricerca Scientifica, 00133, Rome, Italy. bozzi@uniroma2.it
Battistoni
A
A
Sette
M
M
Melino
S
S
Rotilio
G
G
Paci
M
M
D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D004578:Electron Spin Resonance Spectroscopy; D004926:Escherichia coli / Q000201:enzymology*; D066298:In Vitro Techniques; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy; D011489:Protein Denaturation / Q000187:drug effects; D020836:Protein Structure, Quaternary / Q000187:drug effects; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology*; D013482:Superoxide Dismutase / Q000037:antagonists & inhibitors* / Q000737:chemistry*
D046911:Macromolecular Substances; D012967:Sodium Dodecyl Sulfate; D013482:Superoxide Dismutase