Superoxide dismutases are enzymes that protect biological systems against oxidative damage caused by superoxide radicals. In this paper, a detailed characterization is presented on the stability of SmSOD, the dimeric cambialistic superoxide dismutase from the dental pathogenic microorganism Streptococcus mutans, towards temperature and guanidine hydrochloride. Thermal and chemical denaturations were investigated by means of circular dichroism, fourth-derivative UV spectroscopy and fluorescence measurements. Data indicate that SmSOD is endowed with a significant thermostability and that both its thermal and guanidine hydrochloride-induced unfolding processes occur through a three-state model, characterized by a catalytically active dimeric intermediate species. To our knowledge, SmSOD is the smallest known dimeric protein that populates a well-structured active dimeric rather than a monomeric intermediate during unfolding processes.

Identification of an active dimeric intermediate populated during the unfolding process of the cambialistic superoxide dismutase from Streptococcus mutans / Merlino, Antonello; RUSSO KRAUSS, Irene; Rossi, B.; Vergara, Alessandro; De Vendittis, A.; Marco, Salvatore; DE VENDITTIS, Emmanuele; Sica, Filomena. - In: BIOCHIMIE. - ISSN 0300-9084. - 94:(2012), pp. 768-775. [10.1016/j.biochi.2011.11.008]

Identification of an active dimeric intermediate populated during the unfolding process of the cambialistic superoxide dismutase from Streptococcus mutans

MERLINO, ANTONELLO;RUSSO KRAUSS, IRENE;VERGARA, ALESSANDRO;MARCO, SALVATORE;DE VENDITTIS, EMMANUELE;SICA, FILOMENA
2012

Abstract

Superoxide dismutases are enzymes that protect biological systems against oxidative damage caused by superoxide radicals. In this paper, a detailed characterization is presented on the stability of SmSOD, the dimeric cambialistic superoxide dismutase from the dental pathogenic microorganism Streptococcus mutans, towards temperature and guanidine hydrochloride. Thermal and chemical denaturations were investigated by means of circular dichroism, fourth-derivative UV spectroscopy and fluorescence measurements. Data indicate that SmSOD is endowed with a significant thermostability and that both its thermal and guanidine hydrochloride-induced unfolding processes occur through a three-state model, characterized by a catalytically active dimeric intermediate species. To our knowledge, SmSOD is the smallest known dimeric protein that populates a well-structured active dimeric rather than a monomeric intermediate during unfolding processes.
2012
Identification of an active dimeric intermediate populated during the unfolding process of the cambialistic superoxide dismutase from Streptococcus mutans / Merlino, Antonello; RUSSO KRAUSS, Irene; Rossi, B.; Vergara, Alessandro; De Vendittis, A.; Marco, Salvatore; DE VENDITTIS, Emmanuele; Sica, Filomena. - In: BIOCHIMIE. - ISSN 0300-9084. - 94:(2012), pp. 768-775. [10.1016/j.biochi.2011.11.008]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/428483
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