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Efficient proton shuttle makes SazCA an excellent CO2 hydration enzyme.

Shashi Kumar1, Parag A Deshpande1

  • 1Quantum and Molecular Engineering Laboratory, Department of Chemical Engineering, Indian Institute of Technology Kharagpur, Kharagpur, India.

Journal of Biomolecular Structure & Dynamics
|July 21, 2022
PubMed
Summary

Sulfolobus acidocaldarius carbonic anhydrase (SazCA) exhibits exceptional activity due to a higher population of the

Keywords:
Carbonic anhydraseconformationshistidinemolecular dynamics simulationsproton shuttle

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Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Carbonic anhydrases are crucial enzymes catalyzing CO2 hydration.
  • SazCA is the fastest known carbonic anhydrase, showing high activity at elevated temperatures (353 K).
  • Understanding SazCA's molecular basis for high activity is essential for enzyme engineering.

Purpose of the Study:

  • To elucidate the molecular mechanisms behind SazCA's exceptional catalytic activity.
  • To compare SazCA with a related enzyme, SspCA, using molecular dynamics simulations.
  • To identify key residues and conformational states contributing to SazCA's enhanced function.

Main Methods:

  • Molecular dynamics (MD) simulations at various temperatures.
  • Analysis of proton shuttle efficiency between the active site and His64.
  • Root-mean-square fluctuation (RMSF) and hydrogen bond (H-bonds) analysis.

Main Results:

  • Both SazCA and SspCA possess efficient proton shuttle systems involving His64.
  • His64 adopts 'in' and 'out' conformations, with 'in' favoring proton acceptance.
  • SazCA exhibits a significantly higher population of the 'in' conformation compared to SspCA.
  • His2 and His207 in SazCA play a role in stabilizing the 'in' conformation of His64.

Conclusions:

  • The superior activity of SazCA is attributed to a greater prevalence of the proton-accepting 'in' conformation of His64.
  • Specific residues (His2, His207) in SazCA contribute to stabilizing this active conformation.
  • These findings provide insights into the structural basis of high enzyme activity in carbonic anhydrases.