Understanding the Binding and Structures in Model Complexes of Polypeptides and Cofactors.

ABSTRACT: Competitive binding between metal cofactors and functional groups of polypeptides results in a diversity of structures and chemistries in metalloproteins. Herein, we examined elements of this competitive binding using [metal-(auxiliary ligand)-(peptide)] complexes, where the metal-(auxiliary ligand) combinations are Cu^II(terpy)²⁺, Co^III(salen)⁺, and Fe^III(salen)⁺ and the peptides are either the dipeptide arginine-tyrosine (RY) or the tripeptide arginine-tyrosine-glycine (RYG). Structural diversity was established and substantiated via tandem mass spectrometry, with and without peptide derivatization and substitution. All the complexes dissociated to give high abundances of the peptide radical cations, but the structures of t

SUBMITTER: Li Y 

PROVIDER: S-EPMC12464774 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature