title: A diiron protein autogenerates a valine-phenylalanine cross-link.
abstract: 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.
authors: Department of Biochemistry and Biophysics, 2011 Agriculture and Life Sciences Building, Oregon State University, Corvallis, OR 97331, USA.
authors: Richard B
authors: RB
authors: Cooley
authors: Timothy W
authors: TW
authors: Rhoads
authors: Daniel J
authors: DJ
authors: Arp
authors: P Andrew
authors: PA
authors: Karplus
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