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Reversible S-nitrosylation in an engineered azurin.

Shiliang Tian1, Jing Liu1, Ryan E Cowley2

  • 1Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.

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This study demonstrates reversible nitric oxide (NO) binding to copper proteins, providing the first direct evidence of S-nitrosylation in metalloproteins. This discovery offers insights into NO regulation and potential therapeutic applications.

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Area of Science:

  • Biochemistry
  • Bioinorganic Chemistry
  • Metalloprotein Chemistry

Background:

  • S-Nitrosothiols are crucial for nitric oxide (NO) storage and physiological regulation.
  • While NO catalysis by haem proteins is established, direct evidence of S-nitrosylation in copper proteins is lacking.

Purpose of the Study:

  • To provide the first direct evidence of S-nitrosylation in copper proteins.
  • To elucidate the mechanism and structural basis for NO binding to copper-thiolate bonds.
  • To explore the potential of this reaction in biological systems.

Main Methods:

  • Engineered a copper centre in Pseudomonas aeruginosa azurin by modifying its coordination sphere.
  • Tuned the reduction potential by altering secondary coordination sphere interactions.
  • Investigated the reversible insertion of NO into the copper-thiolate bond.

Main Results:

  • Achieved reversible insertion of NO into a copper-thiolate bond in engineered azurin.
  • Provided the first direct evidence of S-nitrosylation of Cu(II)-bound cysteine in metalloproteins.
  • Identified key structural features stabilizing the Cu(I)-S(Cys)NO species.
  • Demonstrated the ability of this reaction to prevent NO inhibition of cytochrome bo3 oxidase.

Conclusions:

  • Established a novel mechanism for NO storage and transport in engineered copper proteins.
  • The findings offer insights into the fundamental chemistry of metalloproteins and NO signaling.
  • This engineered system shows potential for modulating NO-dependent biological processes.