Myoglobin as a model system for designing heme protein based blood substitutes
Y Dou, DH Maillett, RF Eich, JS Olson - Biophysical chemistry, 2002 - Elsevier
The ligand binding properties and resistances to denaturation of> 300 different site-directed
mutants of sperm whale, pig, and human myoglobin have been examined over the past 15
years. This library of recombinant proteins has been used to derive chemical mechanisms
for ligand binding and to examine the factors governing holo-and apoglobin stability. We
have also examined the effects of mutagenesis on the dioxygenation of NO by MbO2 to form
NO3− and metMb. This reaction rapidly detoxifies NO and is a key physiological function of …
mutants of sperm whale, pig, and human myoglobin have been examined over the past 15
years. This library of recombinant proteins has been used to derive chemical mechanisms
for ligand binding and to examine the factors governing holo-and apoglobin stability. We
have also examined the effects of mutagenesis on the dioxygenation of NO by MbO2 to form
NO3− and metMb. This reaction rapidly detoxifies NO and is a key physiological function of …
