Studies on reconstituted myoglobins and hemoglobins. I. role of the heme side chains in the oxygenation of myoglobin

Kuniyasu Kawabe, Kazuhiko Imaizumi, Kiyohiro Imai, Itiro Tyuma, Hisanobu Ogoshi, Takahisa Iwahara, Zen Ichi Yoshida

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

To clarify the functional role of the 2- and 4-side chains of heme in myoglobin oxygenation, we synthesized several new hemins carrying nonnatural side chains at positions 2 and 4, reconstituted myoglobins with them, and investigated their optical, ionization, and oxygen-binding properties. The absorption maxima for most of the reconstituted myoglobins except those reconstituted with hemins having carbonyl groups, no matter whether they are oxy-, deoxy-, or carbon monoxy-form, shifted by at most 20 nm toward shorter wavelengths than protoheme-myoglobin. The absorption spectrum is more affected by resonance effects than by inductive effects of the peripheral side chains of heme. Differences in optical and oxygenation properties between isomeric myoglobins carrying hemes with different side chains at positions 2 and 4 indicate that the 2- and 4-side chains of heme are functionally nonequivalent, as previously shown by Sono and Asakura [(1975) J. Biol. Chem. 250, 5227-5232] for monoformyl-monovinylheme myoglobins. Modification of the 4-side chain exerts greater influence on the oxygen affinity than that of the 2-side chain. The extrapolation method proposed by Sono and Asakura to correct for the protein factor seems to be applicable only as a special case and does not apply to the isomeric myoglobins studied by us. There was not correlation between pK2

Original languageEnglish
Pages (from-to)1703-1712
Number of pages10
JournalJournal of Biochemistry
Volume92
Issue number6
Publication statusPublished - 1982 Oct
Externally publishedYes

Fingerprint

Hemoglobin
Oxygenation
Myoglobin
Heme
Hemoglobins
Oxygen
Extrapolation
Ionization
Absorption spectra
Hemin
Proteins
Wavelength
Carbon
Extrapolation Method
Absorption Spectra
Affine transformation
Absorption
Protein
Factors

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., Imai, K., Tyuma, I., Ogoshi, H., Iwahara, T., & Yoshida, Z. I. (1982). Studies on reconstituted myoglobins and hemoglobins. I. role of the heme side chains in the oxygenation of myoglobin. Journal of Biochemistry, 92(6), 1703-1712.

Studies on reconstituted myoglobins and hemoglobins. I. role of the heme side chains in the oxygenation of myoglobin. / Kawabe, Kuniyasu; Imaizumi, Kazuhiko; Imai, Kiyohiro; Tyuma, Itiro; Ogoshi, Hisanobu; Iwahara, Takahisa; Yoshida, Zen Ichi.

In: Journal of Biochemistry, Vol. 92, No. 6, 10.1982, p. 1703-1712.

Research output: Contribution to journalArticle

Kawabe, K, Imaizumi, K, Imai, K, Tyuma, I, Ogoshi, H, Iwahara, T & Yoshida, ZI 1982, 'Studies on reconstituted myoglobins and hemoglobins. I. role of the heme side chains in the oxygenation of myoglobin', Journal of Biochemistry, vol. 92, no. 6, pp. 1703-1712.
Kawabe K, Imaizumi K, Imai K, Tyuma I, Ogoshi H, Iwahara T et al. Studies on reconstituted myoglobins and hemoglobins. I. role of the heme side chains in the oxygenation of myoglobin. Journal of Biochemistry. 1982 Oct;92(6):1703-1712.
Kawabe, Kuniyasu ; Imaizumi, Kazuhiko ; Imai, Kiyohiro ; Tyuma, Itiro ; Ogoshi, Hisanobu ; Iwahara, Takahisa ; Yoshida, Zen Ichi. / Studies on reconstituted myoglobins and hemoglobins. I. role of the heme side chains in the oxygenation of myoglobin. In: Journal of Biochemistry. 1982 ; Vol. 92, No. 6. pp. 1703-1712.
@article{80371d36c7994e3180eb048f73939923,
title = "Studies on reconstituted myoglobins and hemoglobins. I. role of the heme side chains in the oxygenation of myoglobin",
abstract = "To clarify the functional role of the 2- and 4-side chains of heme in myoglobin oxygenation, we synthesized several new hemins carrying nonnatural side chains at positions 2 and 4, reconstituted myoglobins with them, and investigated their optical, ionization, and oxygen-binding properties. The absorption maxima for most of the reconstituted myoglobins except those reconstituted with hemins having carbonyl groups, no matter whether they are oxy-, deoxy-, or carbon monoxy-form, shifted by at most 20 nm toward shorter wavelengths than protoheme-myoglobin. The absorption spectrum is more affected by resonance effects than by inductive effects of the peripheral side chains of heme. Differences in optical and oxygenation properties between isomeric myoglobins carrying hemes with different side chains at positions 2 and 4 indicate that the 2- and 4-side chains of heme are functionally nonequivalent, as previously shown by Sono and Asakura [(1975) J. Biol. Chem. 250, 5227-5232] for monoformyl-monovinylheme myoglobins. Modification of the 4-side chain exerts greater influence on the oxygen affinity than that of the 2-side chain. The extrapolation method proposed by Sono and Asakura to correct for the protein factor seems to be applicable only as a special case and does not apply to the isomeric myoglobins studied by us. There was not correlation between pK2",
author = "Kuniyasu Kawabe and Kazuhiko Imaizumi and Kiyohiro Imai and Itiro Tyuma and Hisanobu Ogoshi and Takahisa Iwahara and Yoshida, {Zen Ichi}",
year = "1982",
month = "10",
language = "English",
volume = "92",
pages = "1703--1712",
journal = "Journal of Biochemistry",
issn = "0021-924X",
publisher = "Oxford University Press",
number = "6",

}

TY - JOUR

T1 - Studies on reconstituted myoglobins and hemoglobins. I. role of the heme side chains in the oxygenation of myoglobin

AU - Kawabe, Kuniyasu

AU - Imaizumi, Kazuhiko

AU - Imai, Kiyohiro

AU - Tyuma, Itiro

AU - Ogoshi, Hisanobu

AU - Iwahara, Takahisa

AU - Yoshida, Zen Ichi

PY - 1982/10

Y1 - 1982/10

N2 - To clarify the functional role of the 2- and 4-side chains of heme in myoglobin oxygenation, we synthesized several new hemins carrying nonnatural side chains at positions 2 and 4, reconstituted myoglobins with them, and investigated their optical, ionization, and oxygen-binding properties. The absorption maxima for most of the reconstituted myoglobins except those reconstituted with hemins having carbonyl groups, no matter whether they are oxy-, deoxy-, or carbon monoxy-form, shifted by at most 20 nm toward shorter wavelengths than protoheme-myoglobin. The absorption spectrum is more affected by resonance effects than by inductive effects of the peripheral side chains of heme. Differences in optical and oxygenation properties between isomeric myoglobins carrying hemes with different side chains at positions 2 and 4 indicate that the 2- and 4-side chains of heme are functionally nonequivalent, as previously shown by Sono and Asakura [(1975) J. Biol. Chem. 250, 5227-5232] for monoformyl-monovinylheme myoglobins. Modification of the 4-side chain exerts greater influence on the oxygen affinity than that of the 2-side chain. The extrapolation method proposed by Sono and Asakura to correct for the protein factor seems to be applicable only as a special case and does not apply to the isomeric myoglobins studied by us. There was not correlation between pK2

AB - To clarify the functional role of the 2- and 4-side chains of heme in myoglobin oxygenation, we synthesized several new hemins carrying nonnatural side chains at positions 2 and 4, reconstituted myoglobins with them, and investigated their optical, ionization, and oxygen-binding properties. The absorption maxima for most of the reconstituted myoglobins except those reconstituted with hemins having carbonyl groups, no matter whether they are oxy-, deoxy-, or carbon monoxy-form, shifted by at most 20 nm toward shorter wavelengths than protoheme-myoglobin. The absorption spectrum is more affected by resonance effects than by inductive effects of the peripheral side chains of heme. Differences in optical and oxygenation properties between isomeric myoglobins carrying hemes with different side chains at positions 2 and 4 indicate that the 2- and 4-side chains of heme are functionally nonequivalent, as previously shown by Sono and Asakura [(1975) J. Biol. Chem. 250, 5227-5232] for monoformyl-monovinylheme myoglobins. Modification of the 4-side chain exerts greater influence on the oxygen affinity than that of the 2-side chain. The extrapolation method proposed by Sono and Asakura to correct for the protein factor seems to be applicable only as a special case and does not apply to the isomeric myoglobins studied by us. There was not correlation between pK2

UR - http://www.scopus.com/inward/record.url?scp=0020314082&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020314082&partnerID=8YFLogxK

M3 - Article

C2 - 7161256

AN - SCOPUS:0020314082

VL - 92

SP - 1703

EP - 1712

JO - Journal of Biochemistry

JF - Journal of Biochemistry

SN - 0021-924X

IS - 6

ER -