Analogous Effect of Protons and Inositol Hexaphosphate on the Alteration of Structure of Nitrosyl Fetal Human Hemoglobin

M. Chevion*, A. Stern, J. Peisach, W. E. Blumberg, S. Simon

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

We have determined the low temperature EPR spectra and room temperature ligand dissociation rate constants of human NO-hemoglobins F and A as a function of pH and inositol hexaphosphate levels in order to assess the contribution of a quaternary structural equilibrium in the two proteins to their spectral and functional properties. Our results are consistent with an increased stability of a ligated low affinity structure in the fetal protein; the functional properties of this structure appear to be essentially the same in the two hemoglobins, even though its stability relative to a high affinity conformation is different. The pH dependence of the NO dissociation constant in both adult and fetal hemoglobin can be assigned primarily to the pH-dependent equilibria of high and low affinity forms as monitored by EPR.

Original languageEnglish
Pages (from-to)1745-1750
Number of pages6
JournalBiochemistry
Volume17
Issue number9
DOIs
StatePublished - 1978
Externally publishedYes

Fingerprint

Dive into the research topics of 'Analogous Effect of Protons and Inositol Hexaphosphate on the Alteration of Structure of Nitrosyl Fetal Human Hemoglobin'. Together they form a unique fingerprint.

Cite this