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Engineering a Conformationally Switchable Artificial Metalloprotein.

Saman Fatima1, David G Boggs2, Noor Ali3

  • 1Department of Chemistry, University of Illinois Urbana-Champaign, 600 S. Mathews Avenue, Urbana, Illinois61801, United States.

Journal of the American Chemical Society
|November 15, 2022
PubMed
Summary
This summary is machine-generated.

Researchers developed switchable artificial metalloproteins (swArMs) that change shape upon ligand binding. This platform investigates how protein dynamics and metallocofactor activity are interconnected, mimicking natural metalloenzymes.

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Area of Science:

  • Bioinorganic Chemistry
  • Protein Engineering
  • Biophysical Chemistry

Background:

  • Metalloenzymes rely on conformational changes for function, linking protein structure to metallocofactor activity.
  • Existing artificial metalloproteins (ArMs) often lack dynamic flexibility, limiting their ability to model natural systems.
  • Understanding allostery's role in regulating metallocofactor reactivity is crucial for bio-inspired catalyst design.

Purpose of the Study:

  • To engineer conformationally switchable artificial metalloproteins (swArMs) that undergo large-scale structural changes.
  • To investigate the interplay between protein conformational dynamics and metallocofactor electronic structure and reactivity.
  • To establish a platform for studying allosteric regulation of metallocofactor function.

Main Methods:

  • Site-specific incorporation of Cobalt(II)bis(dimethylglyoxime) (Co(dmgH)2(X)) metallocofactors into E. coli glutamine binding protein (GlnBP).
  • Spectroscopic techniques (UV-vis, fluorescence, CD, IR) and mass spectrometry for characterization.
  • X-ray crystallography for structural determination and isothermal titration calorimetry for binding studies.

Main Results:

  • Successfully engineered swArMs with site-specific, stoichiometric Co-S cysteine ligation of the metallocofactor within GlnBP.
  • Demonstrated that allosteric glutamine binding induces significant protein conformational changes.
  • Showed that the protein environment stabilizes the Co-S bond, while conformational changes modulate its dissociation rate.

Conclusions:

  • Developed a novel swArM platform enabling investigation of allostery-driven metallocofactor regulation.
  • Established a direct link between protein conformational dynamics and metallocofactor reactivity in an artificial system.
  • swArMs provide a powerful tool for mimicking and understanding natural metalloenzyme mechanisms.