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How a multimeric macromolecule is affected by divalent salts? Experimental and simulation study.

Fatemeh Janati-Fard1, Mohammad R Housaindokht2, Hassan Monhemi3

  • 1Biophysical Chemistry Laboratory, Department of Chemistry, Faculty of Science, Ferdowsi University of Mashhad, Mashhad, Iran.

International Journal of Biological Macromolecules
|August 8, 2017
PubMed
Summary
This summary is machine-generated.

High salt concentrations, specifically calcium chloride (CaCl2), can inactivate multimeric enzymes like glucose oxidase by altering their structure. Molecular dynamics simulations revealed conformational changes at the active site, explaining this salt-induced enzyme inactivation.

Keywords:
Glucose oxidaseInactivationMD simulationSalt

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Salts are ubiquitous in biological systems and can influence macromolecular behavior.
  • Divalent salts are known to affect protein structure and function at elevated concentrations.
  • Understanding salt effects on enzymes is crucial for both fundamental science and technological applications.

Purpose of the Study:

  • To investigate the impact of divalent salt (CaCl2) on the behavior of a multimeric enzyme, glucose oxidase.
  • To elucidate the structural mechanisms underlying salt-induced enzyme inactivation.
  • To provide a detailed structural analysis of enzyme conformational changes under varying salt conditions.

Main Methods:

  • Experimental treatment of glucose oxidase with varying concentrations of calcium chloride (CaCl2).
  • Molecular dynamics (MD) simulations of the enzyme at different salt concentrations.
  • Analysis of structural properties, including active site and FAD-binding site conformations.

Main Results:

  • Glucose oxidase activity decreases and becomes inactive at high CaCl2 concentrations.
  • MD simulations show conformational changes in the active and FAD-binding sites correlating with enzyme inactivation.
  • Higher salt concentrations lead to an unstable enzyme conformation, consistent with experimental observations.

Conclusions:

  • Divalent salts like CaCl2 can induce structural instability and inactivation in multimeric enzymes.
  • Conformational changes at critical enzyme sites are a key mechanism for salt-induced inactivation.
  • This study provides novel insights into the structural basis of salt effects on multimeric macromolecules.