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Publication Abstract from PubMed

All known internal covalent cross-links in proteins involve functionalized groups having oxygen, nitrogen, or sulfur atoms present to facilitate their formation. Here, we report a carbon-carbon cross-link between two unfunctionalized side chains. This valine-phenyalanine cross-link, produced in an oxygen-dependent reaction, is generated by its own carboxylate-bridged diiron center and serves to stabilize the metallocenter. This finding opens the door to new types of posttranslational modifications, and it demonstrates new catalytic potential of diiron centers.

A diiron protein autogenerates a valine-phenylalanine cross-link.,Cooley RB, Rhoads TW, Arp DJ, Karplus PA Science. 2011 May 20;332(6032):929. PMID:21596985^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.