Int. J. Mol. Sci. 2009, 10(12), 5498-5512; doi:10.3390/ijms10125498
Article

Contributions of the C-Terminal Helix to the Structural Stability of a Hyperthermophilic Fe-Superoxide Dismutase (TcSOD)

1email, 2,* email and 1,* email
Received: 18 November 2009; in revised form: 16 December 2009 / Accepted: 17 December 2009 / Published: 23 December 2009
(This article belongs to the Section Biochemistry, Molecular Biology and Biophysics)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract: Hyperthermophilic superoxide dismutases (SODs) are of particular interest due to their potential industrial importance and scientific merit in studying the molecular mechanisms of protein folding and stability. Compared to the mesophilic SODs, the hyperthermostable Fe-SODs (TcSOD and ApSOD) have an extended C-terminal helix, which forms an additional ion-pairing network. In this research, the role of the extended C-terminus in the structural stability of TcSOD was studied by investigating the properties of two deletion mutants. The results indicated that the ion-pairing network at the C-terminus had limited contributions to the stability of TcSOD against heat- and GdnHClinduced inactivation. The intactness of the C-terminal helix had dissimilar impact on the two stages of TcSOD unfolding induced by guanidinium chloride. The mutations slightly decreased the Gibbs free energy of the dissociation of the tetrameric enzymes, while greatly affected the stability of the molten globule-like intermediate. These results suggested that the additional ion-pairing network mainly enhanced the structural stability of TcSOD by stabilizing the monomers.
Keywords: Fe-superoxide dismutase; hyperthermophilic enzyme; thermostability; ion-pairing network; protein unfolding
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MDPI and ACS Style

Wang, S.; Yan, Y.-B.; Dong, Z.-Y. Contributions of the C-Terminal Helix to the Structural Stability of a Hyperthermophilic Fe-Superoxide Dismutase (TcSOD). Int. J. Mol. Sci. 2009, 10, 5498-5512.

AMA Style

Wang S, Yan Y-B, Dong Z-Y. Contributions of the C-Terminal Helix to the Structural Stability of a Hyperthermophilic Fe-Superoxide Dismutase (TcSOD). International Journal of Molecular Sciences. 2009; 10(12):5498-5512.

Chicago/Turabian Style

Wang, Sha; Yan, Yong-Bin; Dong, Zhi-Yang. 2009. "Contributions of the C-Terminal Helix to the Structural Stability of a Hyperthermophilic Fe-Superoxide Dismutase (TcSOD)." Int. J. Mol. Sci. 10, no. 12: 5498-5512.

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