氰化物介导的构象变化导致硫酸根离子从牛胰腺核糖核酸酶 A 的活性位点移位

IF 2.5 3区生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY

Biochemical and biophysical research communications Pub Date : 2024-10-23 DOI:10.1016/j.bbrc.2024.150868

Nayab Shah , Zeeshan Akbar , Malik Shoaib Ahmad

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引用次数: 0

摘要

核糖核酸酶 A 是一种参与水解核糖核酸的主要水解酶。牛胰腺 RNase A（bpRNase A）的晶体在 pH 值为 5.5 的条件下生长。氰化钠直接加入含晶体的孔中，以评估氰化钠对 bpRNase A 的影响。用氰化钠处理 bpRNase A 晶体会导致硫酸根离子从 bpRNase A 的活性位点移位，而与 Ala-4 结合的硫酸根离子则不受影响。在 bpRNase A 晶体中加入氰化钠不会改变酶的二级结构元素。这项研究的目的是检测氰化物对 bpRNase A 晶体的影响，以及从其活性位点置换硫酸根离子的作用。

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

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.

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来源期刊

Biochemical and biophysical research communications 生物-生化与分子生物学

CiteScore

6.10

自引率

0.00%

发文量

1400

审稿时长

14 days

期刊介绍： Biochemical and Biophysical Research Communications is the premier international journal devoted to the very rapid dissemination of timely and significant experimental results in diverse fields of biological research. The development of the "Breakthroughs and Views" section brings the minireview format to the journal, and issues often contain collections of special interest manuscripts. BBRC is published weekly (52 issues/year).Research Areas now include: Biochemistry; biophysics; cell biology; developmental biology; immunology ; molecular biology; neurobiology; plant biology and proteomics