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

Nayab Shah; Zeeshan Akbar; Malik Shoaib Ahmad

doi:10.1016/j.bbrc.2024.150868

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 Oct 23:736:150868. doi: 10.1016/j.bbrc.2024.150868. Online ahead of print.

Authors

Nayab Shah¹, Zeeshan Akbar², Malik Shoaib Ahmad³

Affiliations

¹ Dr. Panjwani Center for Molecular Medicine and Drug Research, International Center for Chemical and Biological Sciences, University of Karachi, Karachi-75270, Pakistan.
² H. E. J. Research Institute of Chemistry, International Center for Chemical and Biological Sciences, University of Karachi, Karachi, 75270, Pakistan.
³ Dr. Panjwani Center for Molecular Medicine and Drug Research, International Center for Chemical and Biological Sciences, University of Karachi, Karachi-75270, Pakistan; H. E. J. Research Institute of Chemistry, International Center for Chemical and Biological Sciences, University of Karachi, Karachi, 75270, Pakistan. Electronic address: shoaib.hej@gmail.com.

PMID: 39490154
DOI: 10.1016/j.bbrc.2024.150868

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.