Abstract
The rate constants for the association of oxygen and of carbon monoxide with reduced hemoglobin and for the dissociation of oxygen from hemoglobin were studied in a variety of media. All three of these rates were essentially independent of diffusion rate and dielectric constant throughout a wide range. These results are very different from those found for other heme proteins whose rates are diffusion-controlled in very viscous solvents.
The interpretation of the average measured rates described herein in terms of the four rate constants discussed by Gibson and Roughton indicates that our measurements reflect most strongly the constants for the first reacting molecule in each case. For the purposes of these reactions, the reactants may be regarded as neutral molecules.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- GIBSON Q. H., KREUZER F., MEDA E., ROUGHTON F. J. The kinetics of human haemoglobin in solution and in the red cell at 37 degrees C. J Physiol. 1955 Jul 28;129(1):65–89. doi: 10.1113/jphysiol.1955.sp005339. [DOI] [PMC free article] [PubMed] [Google Scholar]
- GIBSON Q. H., ROUGHTON F. J. The kinetics of dissociation of the first oxygen molecule from fully saturated oxyhaemoglobin in sheep blood solutions. Proc R Soc Lond B Biol Sci. 1955 Mar 15;143(912):310–334. doi: 10.1098/rspb.1955.0014. [DOI] [PubMed] [Google Scholar]
- STROTHER G. K., ACKERMAN E., ANTHONY A., STRICKLAND E. H. Effects of altitude acclimatization on rat myoglobin; effect of viscosity and acclimatization on myoglobin reaction rates. Am J Physiol. 1959 Mar;196(3):517–519. doi: 10.1152/ajplegacy.1959.196.3.517. [DOI] [PubMed] [Google Scholar]