Features of the decomposition of thiosulfate nitrosyl iron complex in the presence of hemoglobin and cytochrome c

IF 2.4 3区 化学 Q2 CHEMISTRY, INORGANIC & NUCLEAR
Olesya V. Pokidova , Veronika O. Novikova , Alexander V. Kulikov , Natalia A. Sanina
{"title":"Features of the decomposition of thiosulfate nitrosyl iron complex in the presence of hemoglobin and cytochrome c","authors":"Olesya V. Pokidova ,&nbsp;Veronika O. Novikova ,&nbsp;Alexander V. Kulikov ,&nbsp;Natalia A. Sanina","doi":"10.1016/j.poly.2024.117225","DOIUrl":null,"url":null,"abstract":"<div><p>Nitrosyl complexes of non-heme iron (NICs) are the depot of nitric monoxide (NO) in the body. They nitrosylate heme-containing proteins in the process of decomposition. In this work, we studied the interaction of the thiosulfate complex Na<sub>2</sub>[Fe<sub>2</sub>(S<sub>2</sub>O<sub>3</sub>)<sub>2</sub>(NO)<sub>4</sub>]·4H<sub>2</sub>O (complex 1), as a promising drug agent, with hemoglobin and cytochrome <em>c</em>. It was found that complex 1 and its decomposition products are adsorbed on the surface of oxyhemoglobin, leading to longer NO generation compared to an aqueous buffer solution. In the system with metHb, the accumulation of the product (nitrosyl hemoglobin) occurs only under anaerobic conditions.</p><p>The article also presents experimental data on the nitrosylation of ferro- and ferricytochrome c (cyt c<sup>2+</sup> and cyt c<sup>3+</sup>, respectively) in the presence of complex 1. Cyt c<sup>2+</sup> forms the product (NO)cyt c<sup>2+</sup>, which serves as the “depot” form of NO. This protein has a lesser stabilizing effect on complex 1 compared to hemoglobin. In the system with cyt c<sup>3+</sup>, nitrosylation of protein occurs during mixing, due to the presence of an oxidizing agent K<sub>3</sub>[Fe(CN)<sub>6</sub>].</p></div>","PeriodicalId":20278,"journal":{"name":"Polyhedron","volume":"264 ","pages":"Article 117225"},"PeriodicalIF":2.4000,"publicationDate":"2024-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Polyhedron","FirstCategoryId":"92","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0277538724004017","RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"CHEMISTRY, INORGANIC & NUCLEAR","Score":null,"Total":0}
引用次数: 0

Abstract

Nitrosyl complexes of non-heme iron (NICs) are the depot of nitric monoxide (NO) in the body. They nitrosylate heme-containing proteins in the process of decomposition. In this work, we studied the interaction of the thiosulfate complex Na2[Fe2(S2O3)2(NO)4]·4H2O (complex 1), as a promising drug agent, with hemoglobin and cytochrome c. It was found that complex 1 and its decomposition products are adsorbed on the surface of oxyhemoglobin, leading to longer NO generation compared to an aqueous buffer solution. In the system with metHb, the accumulation of the product (nitrosyl hemoglobin) occurs only under anaerobic conditions.

The article also presents experimental data on the nitrosylation of ferro- and ferricytochrome c (cyt c2+ and cyt c3+, respectively) in the presence of complex 1. Cyt c2+ forms the product (NO)cyt c2+, which serves as the “depot” form of NO. This protein has a lesser stabilizing effect on complex 1 compared to hemoglobin. In the system with cyt c3+, nitrosylation of protein occurs during mixing, due to the presence of an oxidizing agent K3[Fe(CN)6].

Abstract Image

硫代硫酸亚硝基铁复合物在血红蛋白和细胞色素 c 存在下的分解特征
非血红素铁的亚硝基复合物(NIC)是体内一氧化氮(NO)的储存库。它们在分解过程中会亚硝基化含血红素的蛋白质。在这项工作中,我们研究了硫代硫酸盐复合物 Na2[Fe2(S2O3)2(NO)4]-4H2O(复合物 1)与血红蛋白和细胞色素 c 的相互作用,发现复合物 1 及其分解产物吸附在氧合血红蛋白表面,与缓冲水溶液相比,可导致更长时间的一氧化氮生成。文章还介绍了在复合物 1 的存在下,亚铁和铁托色素 c(分别为细胞 c2+ 和细胞 c3+)发生亚硝基化的实验数据。Cyt c2+ 形成的产物 (NO)cyt c2+ 是 NO 的 "仓库 "形式。与血红蛋白相比,这种蛋白质对复合物 1 的稳定作用较小。在含有细胞 c3+ 的系统中,由于存在氧化剂 K3[Fe(CN)6],蛋白质在混合过程中会发生亚硝基化。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Polyhedron
Polyhedron 化学-晶体学
CiteScore
4.90
自引率
7.70%
发文量
515
审稿时长
2 months
期刊介绍: Polyhedron publishes original, fundamental, experimental and theoretical work of the highest quality in all the major areas of inorganic chemistry. This includes synthetic chemistry, coordination chemistry, organometallic chemistry, bioinorganic chemistry, and solid-state and materials chemistry. Papers should be significant pieces of work, and all new compounds must be appropriately characterized. The inclusion of single-crystal X-ray structural data is strongly encouraged, but papers reporting only the X-ray structure determination of a single compound will usually not be considered. Papers on solid-state or materials chemistry will be expected to have a significant molecular chemistry component (such as the synthesis and characterization of the molecular precursors and/or a systematic study of the use of different precursors or reaction conditions) or demonstrate a cutting-edge application (for example inorganic materials for energy applications). Papers dealing only with stability constants are not considered.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信