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Protein metal–nitrosyl motifs

Nitric oxide (NO) is an important signalling molecule involved in a variety of biological processes, but the way in which it interacts with some metalloproteins is not well understood. A collection of articles in this issue reveals how NO binds to proteins containing type-1 copper sites, based on studies with small-molecule mimics and engineered model proteins.

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Editorial

Now we NO p635

doi:10.1038/nchem.2562

Nitric oxide (NO) is an important signalling molecule in biological systems, but it is unclear exactly how it interacts with some metalloproteins. Now, a collection of articles in this issue reveal how NO binds to proteins containing type-1 copper sites.


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News and Views

Metalloproteins: A switch for blue copper proteins? pp639 - 641

Subhra Samanta & Nicolai Lehnert

doi:10.1038/nchem.2561

Nitric oxide (NO) has important functions in all forms of life and serves, for example, as a signalling molecule in mammals. Now, two complementary studies have uncovered how NO binds to blue copper proteins. This research suggests a mechanism by which NO could regulate the activity of blue copper proteins involved in denitrification.

See also: Article by Zhang et al. | Article by Tian et al.


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Articles

A motif for reversible nitric oxide interactions in metalloenzymes pp663 - 669

Shiyu Zhang, Marie M. Melzer, S. Nermin Sen, Nihan Çelebi-Ölçüm & Timothy H. Warren

doi:10.1038/nchem.2502

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NO participates in numerous physiological processes of which many involve the reaction of NO with metalloenzymes to form a metal–nitrosyl (M–NO). Now, addition of NO to models of type 1 Cu sites has provided a fully characterized S-nitrosothiol adduct, [CuI](κ1-N(O)SR), that reversibly loses NO upon purging with an inert gas. These findings suggest a new motif for reversible binding of nitric oxide at bioinorganic metal centres.

See also: News and Views by Samanta & Lehnert

Reversible S-nitrosylation in an engineered azurin pp670 - 677

Shiliang Tian, Jing Liu, Ryan E. Cowley, Parisa Hosseinzadeh, Nicholas M. Marshall, Yang Yu, Howard Robinson, Mark J. Nilges, Ninian J. Blackburn, Edward I. Solomon & Yi Lu

doi:10.1038/nchem.2489

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S-Nitrosylation has emerged as an important pathway for dynamic post-translational regulation of many classes of proteins. Now, the reversible insertion of NO into a copper–thiolate bond has been observed under physiologically relevant conditions using an engineered azurin. DFT calculation indicates that the reaction proceeds via a radical combination mechanism.

See also: News and Views by Samanta & Lehnert


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