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. 1981 Apr;78(4):2292-6.
doi: 10.1073/pnas.78.4.2292.

Mechanisms for excited state relaxation and dissociation of oxymyoglobin and carboxymyoglobin

A H Reynolds, S D Rand, P M Rentzepis

Mechanisms for excited state relaxation and dissociation of oxymyoglobin and carboxymyoglobin

A H Reynolds et al. Proc Natl Acad Sci U S A. 1981 Apr.

Abstract

The dissociation of carboxymyoglobin (MbCO) and oxymyoglobin (MbO2) induced by 530-nm picosecond excitation in the beta band or the 355-nm delta band has been measured by monitoring the absorbance changes at 420 and 440 nm corresponding to ligand-bound and ligand-detached species, respectively. We find that MbO2 and MbCO dissociate with very similar rates, which do not reflect the 30-fold difference between the quantum yields of the two reactions. Kinetic data suggest that a short-lived intermediate is formed that is responsible for the low quantum efficiency of the MbO2 dissociation.

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References

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