Sarnali Sanfui, Manish Jana, Nadia Small, Donald J. Darensbourg, Marcetta Y. Darensbourg
{"title":"一氧化氮在名义铁和Co之间的转移仿生学的腈水合酶活性位点。","authors":"Sarnali Sanfui, Manish Jana, Nadia Small, Donald J. Darensbourg, Marcetta Y. Darensbourg","doi":"10.1007/s00775-024-02092-8","DOIUrl":null,"url":null,"abstract":"<div><p>Related to the inactive form of nitrile hydratase, NHase, that contains Fe(NO) within tripeptide N<sub>2</sub>S<sub>2</sub> binding environment, the NO transfer reactivity of (bis-mercaptoethane diazacycloheptane)Fe(NO) and (bis-mercaptoethane diazadimethylethane)Fe(NO) is compared to Co(NO) analogs. Acceptors of NO include cobalt octaethylporphyrin and the [(N<sub>2</sub>S<sub>2</sub>)M] dimeric precursors in the synthesis of the Fe(NO) and Co(NO) biomimetics. Qualitative rates are augmented by a definitive kinetic study finding that rates of NO transfer from (N<sub>2</sub>S<sub>2</sub>)M(NO) to [(N<sub>2</sub>S<sub>2</sub>)M′]<sub>2</sub> are dependent on M and M′ as well as the hydrocarbon N to N and N to S linkers. We conclude that while Fe(NO) and Co(NO) units are similar in chemical stability, minor first coordination sphere differences may favor the former, Fe(NO), consistent with the discovery of Fe(NO), but not Co(NO), in the as-isolated NHase active site.</p><h3>Graphical abstract</h3>\n<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"30 2","pages":"161 - 168"},"PeriodicalIF":2.7000,"publicationDate":"2025-01-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Nitric oxide transfer between nominal Fe and Co biomimetics of the nitrile hydratase active site\",\"authors\":\"Sarnali Sanfui, Manish Jana, Nadia Small, Donald J. Darensbourg, Marcetta Y. Darensbourg\",\"doi\":\"10.1007/s00775-024-02092-8\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Related to the inactive form of nitrile hydratase, NHase, that contains Fe(NO) within tripeptide N<sub>2</sub>S<sub>2</sub> binding environment, the NO transfer reactivity of (bis-mercaptoethane diazacycloheptane)Fe(NO) and (bis-mercaptoethane diazadimethylethane)Fe(NO) is compared to Co(NO) analogs. Acceptors of NO include cobalt octaethylporphyrin and the [(N<sub>2</sub>S<sub>2</sub>)M] dimeric precursors in the synthesis of the Fe(NO) and Co(NO) biomimetics. Qualitative rates are augmented by a definitive kinetic study finding that rates of NO transfer from (N<sub>2</sub>S<sub>2</sub>)M(NO) to [(N<sub>2</sub>S<sub>2</sub>)M′]<sub>2</sub> are dependent on M and M′ as well as the hydrocarbon N to N and N to S linkers. We conclude that while Fe(NO) and Co(NO) units are similar in chemical stability, minor first coordination sphere differences may favor the former, Fe(NO), consistent with the discovery of Fe(NO), but not Co(NO), in the as-isolated NHase active site.</p><h3>Graphical abstract</h3>\\n<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>\",\"PeriodicalId\":603,\"journal\":{\"name\":\"Journal of Biological Inorganic Chemistry\",\"volume\":\"30 2\",\"pages\":\"161 - 168\"},\"PeriodicalIF\":2.7000,\"publicationDate\":\"2025-01-24\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Biological Inorganic Chemistry\",\"FirstCategoryId\":\"1\",\"ListUrlMain\":\"https://link.springer.com/article/10.1007/s00775-024-02092-8\",\"RegionNum\":3,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Biological Inorganic Chemistry","FirstCategoryId":"1","ListUrlMain":"https://link.springer.com/article/10.1007/s00775-024-02092-8","RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Nitric oxide transfer between nominal Fe and Co biomimetics of the nitrile hydratase active site
Related to the inactive form of nitrile hydratase, NHase, that contains Fe(NO) within tripeptide N2S2 binding environment, the NO transfer reactivity of (bis-mercaptoethane diazacycloheptane)Fe(NO) and (bis-mercaptoethane diazadimethylethane)Fe(NO) is compared to Co(NO) analogs. Acceptors of NO include cobalt octaethylporphyrin and the [(N2S2)M] dimeric precursors in the synthesis of the Fe(NO) and Co(NO) biomimetics. Qualitative rates are augmented by a definitive kinetic study finding that rates of NO transfer from (N2S2)M(NO) to [(N2S2)M′]2 are dependent on M and M′ as well as the hydrocarbon N to N and N to S linkers. We conclude that while Fe(NO) and Co(NO) units are similar in chemical stability, minor first coordination sphere differences may favor the former, Fe(NO), consistent with the discovery of Fe(NO), but not Co(NO), in the as-isolated NHase active site.
期刊介绍：
Biological inorganic chemistry is a growing field of science that embraces the principles of biology and inorganic chemistry and impacts other fields ranging from medicine to the environment. JBIC (Journal of Biological Inorganic Chemistry) seeks to promote this field internationally. The Journal is primarily concerned with advances in understanding the role of metal ions within a biological matrix—be it a protein, DNA/RNA, or a cell, as well as appropriate model studies. Manuscripts describing high-quality original research on the above topics in English are invited for submission to this Journal. The Journal publishes original articles, minireviews, and commentaries on debated issues.
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