Cyanide mediated conformational changes resulted in the displacement of sulfate ion from the active site of bovine pancreatic ribonuclease A

Biochem Biophys Res Commun. 2024 Dec 3:736:150868. doi: 10.1016/j.bbrc.2024.150868. Epub 2024 Oct 23.

Abstract

Ribonuclease A is a major hydrolyzing enzyme involved in the hydrolysis of RNA. The crystals of bovine pancreatic RNase A (bpRNase A) were grown at pH 5.5. The effect of sodium cyanide on bpRNase A was assessed by adding it directly to the crystal containing well. Treating the crystals of bpRNase A with sodium cyanide resulted in the displacement of the sulfate ion from the active site of bpRNase A, while the additional sulfate ion, bound to Ala-4, remained unaffected. The addition of sodium cyanide to bpRNase A crystals did not show change in the secondary structure elements of the enzyme. This study was conducted to check the effect of cyanide on bpRNase A crystals and to displace sulfate ion from its active site.

Keywords: Cyanide; Protein crystallography; Ribonuclease.

MeSH terms

  • Animals
  • Catalytic Domain*
  • Cattle
  • Crystallography, X-Ray
  • Cyanides / chemistry
  • Cyanides / metabolism
  • Protein Conformation*
  • Ribonuclease, Pancreatic* / chemistry
  • Ribonuclease, Pancreatic* / metabolism
  • Sulfates* / chemistry
  • Sulfates* / metabolism

Substances

  • Sulfates
  • Ribonuclease, Pancreatic
  • Cyanides