Infrared evidence for the mode of binding of oxygen to iron of myoglobin from heart muscle

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Abstract

Infrared spectra for oxymyoglobin isolated from bovine heart muscle reveal non-linear end-on binding of O2 to Fe(II) similar, but not identical, to that found for oxyhemoglobins. Difference spectra for 16O2 Mb vs CO Mb and 16O2 Mb vs 18O2 Mb have a band at 1103 cm−1 assigned to bound 16O2. Human oxyhemoglobin A and other hemoglobins exhibited an analogous band at 1107 cm−1. A bonding description with strong covalent bonding between Fe(II) and O2 (i.e.,

) thus applies to oxymyoglobin as well as to oxyhemoglobins. CO Mb and CO HbA give νCO bands at 1944 and 1951 cm−1 respectively with about 10-fold greater intensity than the O-O bands.

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