Olesya V. Pokidova , Veronika O. Novikova , Alexander V. Kulikov , Natalia A. Sanina
{"title":"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","authors":"Olesya V. Pokidova , Veronika O. Novikova , Alexander V. Kulikov , 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":"{\"title\":\"Features of the decomposition of thiosulfate nitrosyl iron complex in the presence of hemoglobin and cytochrome c\",\"authors\":\"Olesya V. Pokidova , Veronika O. Novikova , Alexander V. Kulikov , 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}","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}
Features of the decomposition of thiosulfate nitrosyl iron complex in the presence of hemoglobin and cytochrome c
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].
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.
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