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

Abstract

Bioorganometallic Fe-C bonds are biologically relevant species that may result from the metabolism of natural or synthetic hydrazines. The molecular structures of four new sperm whale mutant myoglobin derivatives with Fe-aryl moieties, namely H64A-tolyl-m, H64A-chlorophenyl-p, H64Q-tolyl-m, and H64Q-chlorophenyl-p, have been determined at 1.7-1.9Å resolution. The structures reveal conformational preferences for the substituted aryls resulting from attachment of the aryl ligands to Fe at the site of net -NHNH₂ release from the precursor hydrazines, and show distal pocket changes that readily accommodate these bulky ligands.

Keywords: Arylhydrazine; Crystal structure; Heme; Iron-carbon; Myoglobin.