Studies on reconstituted myoglobins and hemoglobins. II. role of the heme side chains in the oxygenation of hemoglobin

Kuniyasu Kawabe, Kazuhiko Imaizumi, Zen Ichi Yoshida, Kiyohiro Imai, Itiro Tyuma

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

To clarify the functional role of the 2- and 4-side chains of heme in hemoglobin we prepared several hemins carrying nonnatural side chains at positions 2 and 4, reconstituted human adult hemoglobins with them, and investigated their optical and oxygen binding properties. The absorption maxima for all these reconstituted hemoglobins, no matter whether they are oxy-, deoxy-, or carbon monoxy-form, shifted toward shorter wavelengths than those for protoheme-hemoglobin. As in the case of myoglobin (Kawabe, K., et al. (1982) J. Biochem. 92, 1703-1712), the absorption spectrum is more significantly affected by resonance effects than by the inductive effects of the peripheral heme substituents. Contrary to the case of myo-globins, the spectral difference between pemptoheme-hemoglobin and isopemptoheme-hemoglobin and that between 2-isopropyl-4-vinyl-deuteroheme-hemoglobin and 2-vinyl-4-isopropyldeuteroheme-hemoglobin were very small. All the reconstituted hemoglobins used in this study showed higher oxygen affinity and reduced coopera-tivity in oxygen binding than native hemoglobin. We have shown that the 2- and 4-side chains are functionally nonequivalent and that modification of the 4-side chain exerts greater influence on oxygen affinity than modifying the 2-side chain. The magnitude of the Bohr effect and response to 2, 3-diphosphoglycerate and inositol hexaphosphate were reduced in the reconstituted hemoglobins. We have proposed a stereochemical mechanism based on constraint of heme movement before ligation against the tight distal side of the heme pocket.

Original languageEnglish
Pages (from-to)1713-1722
Number of pages10
JournalJournal of Biochemistry
Volume92
Issue number6
Publication statusPublished - 1982 Oct
Externally publishedYes

Fingerprint

Hemoglobin
Oxygenation
Myoglobin
Heme
Hemoglobins
Oxygen
Affine transformation
2,3-Diphosphoglycerate
Hemin
Phytic Acid
Globins
Absorption Spectra
Ligation
Absorption spectra
Carbon
Absorption
Wavelength

ASJC Scopus subject areas

  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Physiology (medical)
  • Radiology Nuclear Medicine and imaging
  • Molecular Biology
  • Biochemistry

Cite this

Kawabe, K., Imaizumi, K., Yoshida, Z. I., Imai, K., & Tyuma, I. (1982). Studies on reconstituted myoglobins and hemoglobins. II. role of the heme side chains in the oxygenation of hemoglobin. Journal of Biochemistry, 92(6), 1713-1722.

Studies on reconstituted myoglobins and hemoglobins. II. role of the heme side chains in the oxygenation of hemoglobin. / Kawabe, Kuniyasu; Imaizumi, Kazuhiko; Yoshida, Zen Ichi; Imai, Kiyohiro; Tyuma, Itiro.

In: Journal of Biochemistry, Vol. 92, No. 6, 10.1982, p. 1713-1722.

Research output: Contribution to journalArticle

Kawabe, K, Imaizumi, K, Yoshida, ZI, Imai, K & Tyuma, I 1982, 'Studies on reconstituted myoglobins and hemoglobins. II. role of the heme side chains in the oxygenation of hemoglobin', Journal of Biochemistry, vol. 92, no. 6, pp. 1713-1722.
Kawabe, Kuniyasu ; Imaizumi, Kazuhiko ; Yoshida, Zen Ichi ; Imai, Kiyohiro ; Tyuma, Itiro. / Studies on reconstituted myoglobins and hemoglobins. II. role of the heme side chains in the oxygenation of hemoglobin. In: Journal of Biochemistry. 1982 ; Vol. 92, No. 6. pp. 1713-1722.
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