Low-Temperature Thermochromism Marks a Change in Coordination for the Metal Ion in Manganese Superoxide Dismutase†

Biochemistry ◽  
1996 ◽  
Vol 35 (21) ◽  
pp. 6762-6770 ◽  
Author(s):  
Mei M. Whittaker ◽  
James W. Whittaker
Keyword(s):  
Superoxide Dismutase ◽  
Low Temperature ◽  
Metal Ion ◽  
Manganese Superoxide Dismutase ◽  
Manganese Superoxide

scholarly journals Characteristics of a Novel Manganese Superoxide Dismutase of a Hadal Sea Cucumber (Paelopatides sp.) from the Mariana Trench

Marine Drugs ◽  
2019 ◽  
Vol 17 (2) ◽  
pp. 84 ◽  
Author(s):  
Yanan Li ◽  
Xue Kong ◽  
Haibin Zhang
Keyword(s):  
Superoxide Dismutase ◽  
Metal Ion ◽  
Sea Cucumber ◽  
Manganese Superoxide Dismutase ◽  
Guanidine Hydrochloride ◽  
Tween 20 ◽  
Potential Candidate ◽  
Manganese Superoxide ◽  
Divalent Metal Ion ◽  
Triton X

A novel, cold-adapted, and acid-base stable manganese superoxide dismutase (Ps-Mn-SOD) was cloned from hadal sea cucumber Paelopatides sp. The dimeric recombinant enzyme exhibited approximately 60 kDa in molecular weight, expressed activity from 0 °C to 70 °C with an optimal temperature of 0 °C, and resisted wide pH values from 2.2–13.0 with optimal activity (> 70%) at pH 5.0–12.0. The Km and Vmax of Ps-Mn-SOD were 0.0329 ± 0.0040 mM and 9112 ± 248 U/mg, respectively. At tested conditions, Ps-Mn-SOD was relatively stable in divalent metal ion and other chemicals, such as β-mercaptoethanol, dithiothreitol, Tween 20, Triton X-100, and Chaps. Furthermore, the enzyme showed striking stability in 5 M urea or 4 M guanidine hydrochloride, resisted digestion by proteases, and tolerated a high hydrostatic pressure of 100 MPa. The resistance of Ps-Mn-SOD against low temperature, extreme acidity and alkalinity, chemicals, proteases, and high pressure make it a potential candidate in biopharmaceutical and nutraceutical fields.

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