Controlled Ligand Exchange Between Ruthenium Organometallic Cofactor Precursors and a Naive Protein Scaffold Generates Artificial Metalloenzymes Catalysing Transfer Hydrogenation.

ABSTRACT: Many natural metalloenzymes assemble from proteins and biosynthesised complexes, generating potent catalysts by changing metal coordination. Here we adopt the same strategy to generate artificial metalloenzymes (ArMs) using ligand exchange to unmask catalytic activity. By systematically testing Ru^II (η⁶ -arene)(bipyridine) complexes designed to facilitate the displacement of functionalised bipyridines, we develop a fast and robust procedure for generating new enzymes via ligand exchange in a protein that has not evolved to bind such a complex. The resulting metal cofactors form peptidic coordination bonds but also retain a non-biological ligand. Tandem mass spectrometry and ¹⁹ F NMR spectroscopy were used to characterise the organometallic cofactors and ide

SUBMITTER: Biggs GS 

PROVIDER: S-EPMC8251807 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature