Structural and denaturation studies of two mutants of a cold adapted superoxide dismutase point to the importance of electrostatic interactions in protein stability

2014 ◽  
Vol 1844 (3) ◽  
pp. 632-640 ◽  
Author(s):  
Antonello Merlino ◽  
Irene Russo Krauss ◽  
Immacolata Castellano ◽  
Maria Rosaria Ruocco ◽  
Alessandra Capasso ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Protein Stability ◽  
Electrostatic Interactions ◽  
Cold Adapted

Influence of Electrostatic Interactions and Hydrogen Bonding on the Activity of Cyclodextrin-based Superoxide Dismutase Models

2001 ◽  
Vol 13 (5) ◽  
pp. 619-625 ◽  
Author(s):  
Alex Fragoso ◽  
Roberto Cao ◽  
Alicia Díz ◽  
Ileana Sånchez ◽  
Leticia Sånchez
Keyword(s):  
Superoxide Dismutase ◽  
Hydrogen Bonding ◽  
Electrostatic Interactions

Protein stability of mitochondrial superoxide dismutase SOD2 is regulated by USP36

2011 ◽  
Vol 112 (2) ◽  
pp. 498-508 ◽  
Author(s):  
Myung-Sun Kim ◽  
Suresh Ramakrishna ◽  
Key-Hwan Lim ◽  
Jun-Hyun Kim ◽  
Kwang-Hyun Baek
Keyword(s):  
Superoxide Dismutase ◽  
Protein Stability ◽  
Mitochondrial Superoxide ◽  
Mitochondrial Superoxide Dismutase

scholarly journals The Role of Electrostatic Interactions on Klentaq1 Insight for Domain Separation

2012 ◽  
Vol 6 ◽  
pp. BBI.S9390 ◽  
Author(s):  
Santi Nurbaiti ◽  
Muhamad A. Martoprawiro ◽  
Akhmaloka ◽  
Rukman Hertadi
Keyword(s):  
Protein Stability ◽  
Electrostatic Interactions ◽  
Thermal Adaptation ◽  
Atomic Level ◽  
Salt Bridges ◽  
Wild Type ◽  
Interdomain Interactions ◽  
The Relationship ◽  
Domain Separation

We investigated the relationship between the thermostability of Klentaq1 and factors stabilizing interdomain interactions. When thermal adaptation of Klentaq1 was analyzed at the atomic level, the protein was stable at 300 and 350 K. It gradually unfolded at 373 K and almost spontaneously unfolded at 400 K. Domain separation was induced by disrupting electrostatic interactions in two salt bridges formed by Lys354-Glu445 and Asp371-Arg435 on the interface domain. The role of these interactions in protein stability was evaluated by comparing free energy solvation (ΔΔGsolv) between wild type and mutants. Substitution of Asp371 by Glu or Asn, and also Glu445 by Asn resulted in a positive value of ΔΔGsolv, suggesting that mutations destabilized the protein structure. Nevertheless, substitution of Glu445 by Asp gave a negative value to ΔΔGsolv reflecting increasing protein stability. Our results demonstrate that interactions at the interface domains of Klentaq1 are essential factors correlated with the Klentaq1 thermostability.

scholarly journals Electrostatic interactions in the denatured state ensemble: Their effect upon protein folding and protein stability

2008 ◽  
Vol 469 (1) ◽  
pp. 20-28 ◽  
Author(s):  
Jae-Hyun Cho ◽  
Satoshi Sato ◽  
Jia-Cherng Horng ◽  
Burcu Anil ◽  
Daniel P. Raleigh
Keyword(s):  
Protein Folding ◽  
Protein Stability ◽  
Electrostatic Interactions ◽  
Denatured State ◽  
State Ensemble

Electrostatic interactions in Cu, Zn superoxide dismutase

1983 ◽  
Vol 746 (1-2) ◽  
pp. 61-64 ◽  
Author(s):  
Dina Cocco ◽  
Lilia Calabrese ◽  
Alessandro Finazzi-Agrò ◽  
Giuseppe Rotilio
Keyword(s):  
Superoxide Dismutase ◽  
Electrostatic Interactions

scholarly journals Cold-Adapted Glutathione S-Transferases from Antarctic Psychrophilic Bacterium Halomonas sp. ANT108: Heterologous Expression, Characterization, and Oxidative Resistance

Marine Drugs ◽  
2019 ◽  
Vol 17 (3) ◽  
pp. 147 ◽  
Author(s):  
Yanhua Hou ◽  
Chenhui Qiao ◽  
Yifan Wang ◽  
Yatong Wang ◽  
Xiulian Ren ◽  
...  
Keyword(s):  
Low Temperature ◽  
Electrostatic Interactions ◽  
Catalytic Efficiency ◽  
Potential Candidate ◽  
Psychrophilic Bacterium ◽  
Cold Adapted ◽  
E Coli ◽  
Oxidative Resistance ◽  
Arginine Residues ◽  
Glutathione S Transferases

Glutathione S-transferases are one of the most important antioxidant enzymes to protect against oxidative damage induced by reactive oxygen species. In this study, a novel gst gene, designated as hsgst, was derived from Antarctic sea ice bacterium Halomonas sp. ANT108 and expressed in Escherichia coli (E. coli) BL21. The hsgst gene was 603 bp in length and encoded a protein of 200 amino acids. Compared with the mesophilic EcGST, homology modeling indicated HsGST had some structural characteristics of cold-adapted enzymes, such as higher frequency of glycine residues, lower frequency of proline and arginine residues, and reduced electrostatic interactions, which might be in relation to the high catalytic efficiency at low temperature. The recombinant HsGST (rHsGST) was purified to apparent homogeneity with Ni-affinity chromatography and its biochemical properties were investigated. The specific activity of the purified rHsGST was 254.20 nmol/min/mg. The optimum temperature and pH of enzyme were 25 °C and 7.5, respectively. Most importantly, rHsGST retained 41.67% of its maximal activity at 0 °C. 2.0 M NaCl and 0.2% H2O2 had no effect on the enzyme activity. Moreover, rHsGST exhibited its protective effects against oxidative stresses in E. coli cells. Due to its high catalytic efficiency and oxidative resistance at low temperature, rHsGST may be a potential candidate as antioxidant in low temperature health foods.

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