Relationship between Oxygen Affinity and Autoxidation of Myoglobin

Studies using myoglobins reconstituted with a variety of chemically modified heme cofactors revealed that the oxygen affinity and autoxidation reaction rate of the proteins are highly correlated to each other, both decreasing with decreasing the electron density of the heme iron atom. An Fe3+–O2 –-l...

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Published inInorganic chemistry Vol. 51; no. 21; pp. 11955 - 11960
Main Authors Shibata, Tomokazu, Matsumoto, Daichi, Nishimura, Ryu, Tai, Hulin, Matsuoka, Ariki, Nagao, Satoshi, Matsuo, Takashi, Hirota, Shun, Imai, Kiyohiro, Neya, Saburo, Suzuki, Akihiro, Yamamoto, Yasuhiko
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 05.11.2012
Subjects
Animals
Heme - chemistry
Heme - metabolism
Kinetics
Ligands
Myoglobin - chemistry
Myoglobin - metabolism
Oxidation-Reduction
Oxygen - chemistry
Oxygen - metabolism
Spectrophotometry, Ultraviolet
Whales
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Summary:Studies using myoglobins reconstituted with a variety of chemically modified heme cofactors revealed that the oxygen affinity and autoxidation reaction rate of the proteins are highly correlated to each other, both decreasing with decreasing the electron density of the heme iron atom. An Fe3+–O2 –-like species has been expected for the Fe2+–O2 bond in the protein, and the electron density of the heme iron atom influences the resonance process between the two forms. A shift of the resonance toward the Fe2+–O2 form results in lowering of the O2 affinity due to an increase in the O2 dissociation rate. On the other hand, a shift of the resonance toward the Fe3+–O2 –-like species results in acceleration of the autoxidation through increasing H+ affinity of the bound ligand.
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content type line 23
ISSN:0020-1669
1520-510X
DOI:10.1021/ic301848t