Solution-state proton nuclear magnetic resonance (NMR) spectroscopic studies of the active site of myoglobins in various ligated states: Models for macromolecule-substrate binding and advancement of paramagnetic NMR techniques.

摘要

yoglobin (Mb), an oxygen-binding protein found in muscle, is the classical model for hemoglobin (Hb). Because it is monomeric and non-allosteric, Mb is more easily studied by nuclear magnetic resonance (NMR) than is Hb. Mb serves to store oxygen and to enhance oxygen transport to the mitochondria during oxidation of cell nutrients. A less well-known, albeit highly significant, role of Mb is the involvement of its oxidized form in a redox cycle in the presence of a reducing agent, acting as a peroxidase. This is of chemical and clinical interest because of the potential for improvement in reperfusion following ischemia (hypoxia) and myocardial surgery.;Direct interactions of environmentally hazardous organic molecules have been shown to adversely affect the functions of hemoproteins. ;This research accomplished the goal of depicting the dynamism of ligand binding in Mbs with solution-state