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Activated manganese(IV) oxide can selectively oxidize allylic and benzylic alcohols via a radical intermediate mechanism. Primary allylic alcohols are oxidized to aldehydes, while secondary allylic alcohols yield ketones. The redox reaction of potassium permanganate with an Mn(II) salt such as manganese sulfate (under either alkaline or acidic conditions), followed by thorough drying, yields the oxidizing agent: activated MnO2. While MnO2 is insoluble in the solvents used for the reaction, the...
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EDTA titrations are usually carried out in highly basic conditions, where the fully deprotonated form of EDTA, Y4−, actively complexes with the free metal ions in the solution. Several metal ions precipitate as hydrous oxide (hydroxides, oxides, or oxyhydroxides) under these conditions, lowering the concentration of free metal ions in the solution. For this reason, auxiliary complexing agents or ligands such as ammonia, tartrate, citrate, or triethanolamine are used in EDTA titrations to...
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A cold-active esterase enhances mesophilic properties through Mn2+ binding.

Alessandro Marchetti1, Marco Orlando1,2, Marco Mangiagalli1

  • 1Department of Biotechnology and Biosciences, University of Milano-Bicocca, Italy.

The FEBS Journal
|October 21, 2022
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Summary

Manganese ion (Mn2+) binding surprisingly enhances the thermal stability and catalytic efficiency of a cold-active esterase from Antarctic bacteria. This atypical strategy may help cold-active enzymes function better in varying temperatures.

Keywords:
GDSx esterasescold adaptationenzyme stabilitypsychrophilic enzymestemperature adaptation

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Psychrophilic organisms produce cold-active enzymes crucial for adaptation to cold environments.
  • These enzymes possess high activity at low temperatures but are structurally flexible and thermolabile.
  • The role of metal ions in modulating enzyme flexibility and stability is poorly understood.

Purpose of the Study:

  • To investigate the role of manganese ion (Mn2+) binding in the thermal adaptation of a cold-active esterase (M-Est) from Marinomonas sp. ef1.
  • To understand how Mn2+ affects the structural flexibility, thermal stability, and catalytic efficiency of M-Est.

Main Methods:

  • Biochemical assays to determine enzyme activity and stability.
  • Computational analyses, including molecular dynamics simulations.
  • Identification of the Mn2+ binding site and analysis of conformational changes.

Main Results:

  • M-Est, a thermolabile esterase with optimal activity at 5°C, binds Mn2+ at a surface-exposed site near the active site.
  • Mn2+ binding induces local conformational changes, surprisingly improving both thermal stability (Tm = 31.7°C) and catalytic efficiency.
  • The Mn2+ binding site is conserved in related psychrophilic and psychrotolerant enzymes.

Conclusions:

  • Mn2+ binding represents an atypical but potentially effective strategy to enhance the performance of cold-active enzymes.
  • This finding offers insights into the mechanisms of thermal adaptation in extremophilic organisms.
  • Understanding metal ion interactions can guide the engineering of enzymes for specific temperature conditions.