Direct Evidence for a Hydrogen Bond to Bound Dioxygen in a Myoglobin/Hemoglobin Model System and in Cobalt Myoglobin by Pulse‐EPR Spectroscopy

Abstract

Hydrogen bond revealed: In a cobalt(II) porphyrin complex which serves as a model for the dioxygen binding site of myoglobin (Mb) and hemoglobin, a distal hydrogen bond to the bound O2 was identified and characterized by pulse ENDOR spectroscopy. A similar but stronger hydrogen bond was revealed with the same methods in natural Co-Mb-O2.