Protein metal–nitrosyl motifs

Content

• Now we NO

  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.

  Editorial21 Jun 2016 Nature Chemistry
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  A switch for blue copper proteins?

  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.

  • Subhra Samanta
  • Nicolai Lehnert

  News & Views21 Jun 2016 Nature Chemistry
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  A motif for reversible nitric oxide interactions in metalloenzymes

  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, [Cu^I](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.

  • Shiyu Zhang
  • Marie M. Melzer
  • Timothy H. Warren

  Article25 Apr 2016 Nature Chemistry
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  Reversible S-nitrosylation in an engineered azurin

  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.

  • Shiliang Tian
  • Jing Liu
  • Yi Lu

  Article25 Apr 2016 Nature Chemistry