期刊
NATURE CHEMISTRY
卷 8, 期 7, 页码 663-669出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nchem.2502
关键词
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资金
- US National Science Foundation [CHE-1459090]
- Purdue University Department of Chemistry
- Vorisek Endowment at Georgetown University
- TUBITAK ULAKBIM High Performance and Grid Computing Center (TRUBA, Turkey)
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1459090] Funding Source: National Science Foundation
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1337975] Funding Source: National Science Foundation
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 Fe2+ centres of soluble guanylate cyclase or cytochrome c oxidase. However, some copper electron-transfer proteins that bear a type 1 Cu site (His(2)Cu-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](kappa(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.
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