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. 1963 Nov;3(6):493–505. doi: 10.1016/s0006-3495(63)86834-4

Reaction of Oxyhemoglobin with Carbon Monoxide

Eugene Ackerman, Robert L Berger
PMCID: PMC1366464  PMID: 14070363

Abstract

The reaction of oxyhemoglobin and carbon monoxide was studied kinetically at pH 7.8 in a variety of suspending media. The dielectric constant of the suspending media, as well as the viscosity (and hence the Fick diffusion coefficients), was varied with the use of glycine, glycerol, and sucrose. The results showed that the reaction was unaltered by the various additions to the media, provided that the pO2 and the concentration of carbon monoxide were held constant. Since the concentration of oxygen varies from medium to medium at constant pO2 while the pCO varies at constant concentration of carbon monoxide, the differences in the reactions with oxygen and carbon monoxide were emphasized. The lack of variation of the rate constants with changes in dielectric constant can be interpreted as indicating that electrostatic effects are unimportant in this reaction.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ACKERMAN E., BERGER R. L., BLAIR W. L., STROTHER G. K. THE REACTIONS OF HEMOGLOBIN IN VARIOUS MEDIA. Biophys J. 1963 Nov;3:469–478. doi: 10.1016/s0006-3495(63)86832-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. ACKERMAN E. Effect of dielectric changes on catalase reaction rates. Biochim Biophys Acta. 1961 Jun 10;50:181–183. doi: 10.1016/0006-3002(61)91080-0. [DOI] [PubMed] [Google Scholar]
  3. FARWELL R. W., ACKERMAN E. EFFECT OF PHYSICAL FACTORS ON REACTIONS OF HORSE-RADISH PEROXIDASE COMPLEXES WITH REDUCED CYTOCHROME C. Biophys J. 1963 Nov;3:479–491. doi: 10.1016/s0006-3495(63)86833-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. GOMEZ D. M. Considerations of oxygen-hemoglobin equilibrium in the physiological state. Am J Physiol. 1961 Jan;200:135–142. doi: 10.1152/ajplegacy.1961.200.1.135. [DOI] [PubMed] [Google Scholar]
  5. KEILIN D., HARTREE E. F. Effect of drying upon the absorption spectra of haemoglobin and its derivatives. Nature. 1952 Jul 26;170(4317):161–162. doi: 10.1038/170161a0. [DOI] [PubMed] [Google Scholar]
  6. NICOLSON P., ROUGHTON F. J. W. A theoretical study of the influence of diffusion and chemical reaction velocity on the rate of exchange of carbon monoxide and oxygen between the red blood corpuscle and the surrounding fluid. Proc R Soc Lond B Biol Sci. 1951 Jun;138(891):241–264. doi: 10.1098/rspb.1951.0020. [DOI] [PubMed] [Google Scholar]
  7. ROUGHTON F. J. The equilibrium between carbon monoxide and sheep haemoglobin at very high percentage saturations. J Physiol. 1954 Nov 29;126(2):359–383. doi: 10.1113/jphysiol.1954.sp005215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]

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