Mechanisms for excited state relaxation and dissociation of oxymyoglobin and carboxymyoglobin. Academic Article

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.

authors

• Rentzepis, Peter

published proceedings

• Proc Natl Acad Sci U S A

author list (cited authors)

• Reynolds, A. H., Rand, S. D., & Rentzepis, P. M.

citation count

• 36

complete list of authors

• Reynolds, AH||Rand, SD||Rentzepis, PM

publication date

• April 1981

publisher

• Proceedings of the National Academy of Sciences  Publisher

published in

• Proceedings of the National Academy of Sciences of the United States of America  Journal

keywords

• Animals
• Kinetics
• Light
• Myoglobin
• Oxygen
• Protein Binding
• Spectrum Analysis
• Whales

PubMed Central ID

• 6941287

Digital Object Identifier (DOI)

• 10.1073/pnas.78.4.2292

start page

• 2292

end page

• 2296

volume

• 78

issue

• 4

URL

• http%3A%2F%2Fdx.doi.org%2F10.1073%2Fpnas.78.4.2292