Spin equilibrium in human methemoglobin: Effects of inositol hexaphosphate and bezafibrate as measured by resonance Raman spectroscopy

Robert W. Noble, Alice DeYoung, Denis L. Rousseau

Research output: Contribution to journalArticle

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Abstract

The spin equilibria of several derivatives of human methemoglobin were probed by resonance Raman scattering. The intensity of lines in the Raman spectrum gives a measure of the high-spin (S = 5/2) to low-spin (S = 1/2) ratio which agrees well with the spin equilibria determined from direct magnetic susceptibility measurements. The addition of bezafibrate (BZF) to methemoglobin in the absence of organic phosphate, IHP, has very little effect on the spin equilibrium, whereas in the presence of IHP it augments the change in spin significantly. When both IHP and BZF are added to the mixed-spin derivatives (H2O, SCN-, OCN-, and NO2-) of human methemoglobin, the spin equilibrium is shifted toward higher spin by about 700 cal/mol, similar to the spin change detected in derivatives of carp methemoglobin upon addition of IHP alone. These data support a general mechanism for the allosteric transition in which a constant fraction of the cooperative energy (≈20%) is detected at the heme of the ferric ligand-bound forms.

Original languageEnglish (US)
Pages (from-to)5293-5297
Number of pages5
JournalBiochemistry
Volume28
Issue number12
StatePublished - 1989
Externally publishedYes

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Bezafibrate
Methemoglobin
Phytic Acid
Raman Spectrum Analysis
Raman spectroscopy
Derivatives
Raman scattering
Carps
Organophosphates
Magnetic susceptibility
Heme
Ligands

ASJC Scopus subject areas

  • Biochemistry

Cite this

Spin equilibrium in human methemoglobin : Effects of inositol hexaphosphate and bezafibrate as measured by resonance Raman spectroscopy. / Noble, Robert W.; DeYoung, Alice; Rousseau, Denis L.

In: Biochemistry, Vol. 28, No. 12, 1989, p. 5293-5297.

Research output: Contribution to journalArticle

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AB - The spin equilibria of several derivatives of human methemoglobin were probed by resonance Raman scattering. The intensity of lines in the Raman spectrum gives a measure of the high-spin (S = 5/2) to low-spin (S = 1/2) ratio which agrees well with the spin equilibria determined from direct magnetic susceptibility measurements. The addition of bezafibrate (BZF) to methemoglobin in the absence of organic phosphate, IHP, has very little effect on the spin equilibrium, whereas in the presence of IHP it augments the change in spin significantly. When both IHP and BZF are added to the mixed-spin derivatives (H2O, SCN-, OCN-, and NO2-) of human methemoglobin, the spin equilibrium is shifted toward higher spin by about 700 cal/mol, similar to the spin change detected in derivatives of carp methemoglobin upon addition of IHP alone. These data support a general mechanism for the allosteric transition in which a constant fraction of the cooperative energy (≈20%) is detected at the heme of the ferric ligand-bound forms.

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