Organometallic myoglobins: Formation of Fe-carbon bonds and distal pocket effects on aryl ligand conformations

Bioorganometallic Fe-aryl derivatives of myoglobin mutants (H64A and H64Q) have been prepared from their myoglobin FeIII(H2O) precursors and arylhydrazines. Their X-ray crystal structures reveal that the C-atom bound to the hydrazine is what attaches to Fe, and that the aryl ligands are accommodated by conformational changes in the distal pockets.53