Discriminatory Binding of Carbon Monoxide versus Dioxygen within Heme Proteins and Model Hemes
David, S., David Dolphin, and James, B.R.,
Frontiers in Bioinorganic Chemistry Ed. Xavier, A.V., VCH Verlagsgesellschaft, Weinheim
A review and discussion with 52 references. Although reversible binding of O2 and CO to heme proteins occurs at the Fe atom, the steric and electronic controls provided by the protein play major roles in the nature and extent of coordination. Both proximal and distal effects are known in the complex protein environments. To separately understand these effects, model Fe porphyrins have been prepared and their ligand binding examined. Observations made with model systems containing a cap on one face of the porphyrin when the polarity in the vicinity of the Fe-ligand binding site is changed are compared.