دورية أكاديمية
A motif for reversible nitric oxide interactions in metalloenzymes.
العنوان: | A motif for reversible nitric oxide interactions in metalloenzymes. |
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المؤلفون: | Zhang S; Department of Chemistry, Georgetown University, Box 571227, Washington, DC 20057, USA., Melzer MM; Department of Chemistry, Georgetown University, Box 571227, Washington, DC 20057, USA., Sen SN; Department of Chemical Engineering, Yeditepe University, Istanbul 34755, Turkey., Çelebi-Ölçüm N; Department of Chemical Engineering, Yeditepe University, Istanbul 34755, Turkey., Warren TH; Department of Chemistry, Georgetown University, Box 571227, Washington, DC 20057, USA.; Department of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, Indiana 47907, USA. |
المصدر: | Nature chemistry [Nat Chem] 2016 Jul; Vol. 8 (7), pp. 663-9. Date of Electronic Publication: 2016 Apr 25. |
نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
اللغة: | English |
بيانات الدورية: | Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101499734 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1755-4349 (Electronic) Linking ISSN: 17554330 NLM ISO Abbreviation: Nat Chem Subsets: MEDLINE |
أسماء مطبوعة: | Original Publication: London : Nature Pub. Group |
مواضيع طبية MeSH: | Metalloproteins/*chemistry , Nitric Oxide/*chemistry , Nitric Oxide/*metabolism, Borates/chemistry ; Copper/chemistry ; Metalloproteins/metabolism ; Pyrazoles/chemistry |
مستخلص: | Nitric oxide (NO) participates in numerous biological processes, such as signalling in the respiratory system and vasodilation in the cardiovascular system. Many metal-mediated processes involve direct reaction of NO to form a metal-nitrosyl (M-NO), as occurs at the Fe(2+) centres of soluble guanylate cyclase or cytochrome c oxidase. However, some copper electron-transfer proteins that bear a type 1 Cu site (His2Cu-Cys) reversibly bind NO by an unknown motif. Here, we use model complexes of type 1 Cu sites based on tris(pyrazolyl)borate copper thiolates [Cu(II)]-SR to unravel the factors involved in NO reactivity. Addition of NO provides the fully characterized S-nitrosothiol adduct [Cu(I)](κ(1)-N(O)SR), which reversibly loses NO on purging with an inert gas. Computational analysis outlines a low-barrier pathway for the capture and release of NO. These findings suggest a new motif for reversible binding of NO at bioinorganic metal centres that can interconvert NO and RSNO molecular signals at copper sites. |
التعليقات: | Comment in: Nat Chem. 2016 Jun 21;8(7):635. (PMID: 27325084) |
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سلسلة جزيئية: | PubChem-Substance 312811021; 312811022; 312811023; 312811024; 312811025; 312811026; 312811027; 312811028; 312811029; 312811030; 312811031; 312811032; 312811033; 312811034; 312811035; 312811036 |
المشرفين على المادة: | 0 (Borates) 0 (Metalloproteins) 0 (Pyrazoles) 0 (tris(pyrazolyl)borate) 31C4KY9ESH (Nitric Oxide) 789U1901C5 (Copper) |
تواريخ الأحداث: | Date Created: 20160622 Date Completed: 20180817 Latest Revision: 20181113 |
رمز التحديث: | 20221213 |
DOI: | 10.1038/nchem.2502 |
PMID: | 27325092 |
قاعدة البيانات: | MEDLINE |
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