Abstract
The tertiary and quaternary structures of many proteins are stabilized by strong covalent forces, of which disulfide bonds are the most well known. A new type of intramolecular and intermolecular covalent bond has been recently reported, consisting of the Lys and Cys side-chains linked by an oxygen atom (NOS). These post-translational modifications are widely distributed amongst proteins, and are formed under oxidative conditions. Similar linkages are observed during antibiotic biosynthesis, where hydroxylamine intermediates are tethered to the sulfur of enzyme active site Cys residues. These linkages open the way to understanding protein structure and function, give new insights into enzyme catalysis and natural product biosynthesis, and offer new strategies for drug design.
| Original language | English |
|---|---|
| Pages (from-to) | 9463-9471 |
| Number of pages | 9 |
| Journal | Chemical communications (Cambridge, England) |
| Volume | 60 |
| Issue number | 71 |
| Early online date | 2 Aug 2024 |
| DOIs | |
| Publication status | Published - 14 Sept 2024 |
Bibliographical note
Invited article to the 60th anniversary collection of ChemComm. Designated as a Hot Paper. An image of research was used as the front cover of the issue.Data Availability Statement
No primary research results, software or code are included, and no new data were generated or analysed.Funding
No specific funding was obtained for this highlight.