Generation, Characterization, and Tunable Reactivity of Organometallic Fragments Bound to a Protein Ligand.

ABSTRACT: Organotransition metal complexes catalyze important synthetic transformations, and the development of these systems has rested on the detailed understanding of the structures and elementary reactions of discrete organometallic complexes bound to organic ligands. One strategy for the creation of new organometallic systems is to exploit the intricate and highly structured ligands found in natural metalloproteins. We report the preparation and characterization of discrete rhodium and iridium fragments bound site-specifically in a κ(2)-fashion to the protein carbonic anhydrase as a ligand. The reactions of apo human carbonic anhydrase with [Rh(nbd)2]BF4 or [M(CO)2(acac)] (M=Rh, Ir) form proteins containing Rh or Ir with organometallic ligands. A colorimetric assay was developed to quantify rap

SUBMITTER: Key HM 

PROVIDER: S-EPMC11620536 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature