دورية أكاديمية

A motif for reversible nitric oxide interactions in metalloenzymes.

التفاصيل البيبلوغرافية
العنوان: A motif for reversible nitric oxide interactions in metalloenzymes.
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