The Molecular Mechanism of Autoxidation for Myoglobin and Hemoglobin: A Venerable Puzzle
Shikama, K.
Chemical Reviews 98(4): 1357-1374
1998
ISSN/ISBN: 0009-2665 PMID: 11848936 Document Number: 7734
The transport and storage of molecular oxygen by hemoglobin (Hb) and by myoglobin (Mb) are essential to life. The iron(II)-dioxygen bond in these heme proteins plays a vital role in their physiology. Studies of these proteins range from examinations of physical-chemical properties dependent on electronic structure, to investigations of stability as a function of oxygen supply.1 Among these, stability properties are of particular importance in vivo. Like all known dioxygen carriers synthesized so far with transition metals, the oxygenated forms of myoglobin and hemoglobin are oxidized easily to their ferric met forms, which cannot be oxygenated and are therefore physiologically inactive. The mechanistic details of this autoxidation reaction, which are of clinical, as well as of chemical, interest, have long been investigated by a number of authors, but a full understanding of the reaction has not been reached.
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