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.



Now we NO p635


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.


News and Views

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

Subhra Samanta & Nicolai Lehnert


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.



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


no alt info

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


no alt info

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

Extra navigation