Properties of and oxygen binding by albumin-tetraphenylporphyrinatoiron(II) derivative complexes

Eishun Tsuchida, Katsutoshi Ando, Hiromitsu Maejima, Noriyuki Kawai, Teruyuki Komatsu, Shinji Takeoka, Hiroyuki Nishide

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

A hydrophobic tetraphenylporphyrinatoiron(II) derivative bearing a covalently bound axial imidazole [Fe(II)P] was efficiently and noncovalently bound into human serum albumin (HSA) up to an average of eight Fe(II)P molecules per HSA molecule. The aqueous solutions of the HSA-Fe(II)P complex provided a reversible and relatively stable oxygen adduct under physiological conditions (pH 7.4 and 37 °C). The half-life of the oxygen adduct (τ( 1/4 )) was 1 h at 37 °C in an air atmosphere. With Fe(II)-TpivPP (the so-called 'picket-fence heme') having no axial base, an oxygenated HSA-Fe(II)TpivPP complex was obtained using a 20-fold molar excess of 1,2-dimethylimidazole, but the τ( 1/4 ) was very short (ca. 10 min at 37 °C). The oxygen affinity [P( 1/4 )(O2)] and oxygen transporting efficiency (OTE) of HSA-Fe(II)P at 37 °C were 30 Torr and 22%, respectively. Furthermore, the oxygen-binding and dissociation rate constants (k(on) and ko(off)) are extremely high in comparison with those of hemoglobin. The HSA molecule binding eight Fe(II)P molecules can transport about 3.4 mL/dL of oxygen under physiological conditions, corresponding to about 60 % of the oxygen transporting amount of human blood.

Original languageEnglish
Pages (from-to)534-538
Number of pages5
JournalBioconjugate Chemistry
Volume8
Issue number4
DOIs
Publication statusPublished - 1997 Jul

Fingerprint

Albumins
Serum Albumin
Oxygen
Derivatives
Molecules
Bearings (structural)
Fences
Hemoglobin
imidazole
Heme
Atmosphere
Rate constants
Blood
Half-Life
Hemoglobins
Air

ASJC Scopus subject areas

  • Chemistry(all)
  • Organic Chemistry
  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

Properties of and oxygen binding by albumin-tetraphenylporphyrinatoiron(II) derivative complexes. / Tsuchida, Eishun; Ando, Katsutoshi; Maejima, Hiromitsu; Kawai, Noriyuki; Komatsu, Teruyuki; Takeoka, Shinji; Nishide, Hiroyuki.

In: Bioconjugate Chemistry, Vol. 8, No. 4, 07.1997, p. 534-538.

Research output: Contribution to journalArticle

Tsuchida, Eishun ; Ando, Katsutoshi ; Maejima, Hiromitsu ; Kawai, Noriyuki ; Komatsu, Teruyuki ; Takeoka, Shinji ; Nishide, Hiroyuki. / Properties of and oxygen binding by albumin-tetraphenylporphyrinatoiron(II) derivative complexes. In: Bioconjugate Chemistry. 1997 ; Vol. 8, No. 4. pp. 534-538.
@article{8f3b18398d3d4bdf9200db8b34fc2c5d,
title = "Properties of and oxygen binding by albumin-tetraphenylporphyrinatoiron(II) derivative complexes",
abstract = "A hydrophobic tetraphenylporphyrinatoiron(II) derivative bearing a covalently bound axial imidazole [Fe(II)P] was efficiently and noncovalently bound into human serum albumin (HSA) up to an average of eight Fe(II)P molecules per HSA molecule. The aqueous solutions of the HSA-Fe(II)P complex provided a reversible and relatively stable oxygen adduct under physiological conditions (pH 7.4 and 37 °C). The half-life of the oxygen adduct (τ( 1/4 )) was 1 h at 37 °C in an air atmosphere. With Fe(II)-TpivPP (the so-called 'picket-fence heme') having no axial base, an oxygenated HSA-Fe(II)TpivPP complex was obtained using a 20-fold molar excess of 1,2-dimethylimidazole, but the τ( 1/4 ) was very short (ca. 10 min at 37 °C). The oxygen affinity [P( 1/4 )(O2)] and oxygen transporting efficiency (OTE) of HSA-Fe(II)P at 37 °C were 30 Torr and 22{\%}, respectively. Furthermore, the oxygen-binding and dissociation rate constants (k(on) and ko(off)) are extremely high in comparison with those of hemoglobin. The HSA molecule binding eight Fe(II)P molecules can transport about 3.4 mL/dL of oxygen under physiological conditions, corresponding to about 60 {\%} of the oxygen transporting amount of human blood.",
author = "Eishun Tsuchida and Katsutoshi Ando and Hiromitsu Maejima and Noriyuki Kawai and Teruyuki Komatsu and Shinji Takeoka and Hiroyuki Nishide",
year = "1997",
month = "7",
doi = "10.1021/bc9700906",
language = "English",
volume = "8",
pages = "534--538",
journal = "Bioconjugate Chemistry",
issn = "1043-1802",
publisher = "American Chemical Society",
number = "4",

}

TY - JOUR

T1 - Properties of and oxygen binding by albumin-tetraphenylporphyrinatoiron(II) derivative complexes

AU - Tsuchida, Eishun

AU - Ando, Katsutoshi

AU - Maejima, Hiromitsu

AU - Kawai, Noriyuki

AU - Komatsu, Teruyuki

AU - Takeoka, Shinji

AU - Nishide, Hiroyuki

PY - 1997/7

Y1 - 1997/7

N2 - A hydrophobic tetraphenylporphyrinatoiron(II) derivative bearing a covalently bound axial imidazole [Fe(II)P] was efficiently and noncovalently bound into human serum albumin (HSA) up to an average of eight Fe(II)P molecules per HSA molecule. The aqueous solutions of the HSA-Fe(II)P complex provided a reversible and relatively stable oxygen adduct under physiological conditions (pH 7.4 and 37 °C). The half-life of the oxygen adduct (τ( 1/4 )) was 1 h at 37 °C in an air atmosphere. With Fe(II)-TpivPP (the so-called 'picket-fence heme') having no axial base, an oxygenated HSA-Fe(II)TpivPP complex was obtained using a 20-fold molar excess of 1,2-dimethylimidazole, but the τ( 1/4 ) was very short (ca. 10 min at 37 °C). The oxygen affinity [P( 1/4 )(O2)] and oxygen transporting efficiency (OTE) of HSA-Fe(II)P at 37 °C were 30 Torr and 22%, respectively. Furthermore, the oxygen-binding and dissociation rate constants (k(on) and ko(off)) are extremely high in comparison with those of hemoglobin. The HSA molecule binding eight Fe(II)P molecules can transport about 3.4 mL/dL of oxygen under physiological conditions, corresponding to about 60 % of the oxygen transporting amount of human blood.

AB - A hydrophobic tetraphenylporphyrinatoiron(II) derivative bearing a covalently bound axial imidazole [Fe(II)P] was efficiently and noncovalently bound into human serum albumin (HSA) up to an average of eight Fe(II)P molecules per HSA molecule. The aqueous solutions of the HSA-Fe(II)P complex provided a reversible and relatively stable oxygen adduct under physiological conditions (pH 7.4 and 37 °C). The half-life of the oxygen adduct (τ( 1/4 )) was 1 h at 37 °C in an air atmosphere. With Fe(II)-TpivPP (the so-called 'picket-fence heme') having no axial base, an oxygenated HSA-Fe(II)TpivPP complex was obtained using a 20-fold molar excess of 1,2-dimethylimidazole, but the τ( 1/4 ) was very short (ca. 10 min at 37 °C). The oxygen affinity [P( 1/4 )(O2)] and oxygen transporting efficiency (OTE) of HSA-Fe(II)P at 37 °C were 30 Torr and 22%, respectively. Furthermore, the oxygen-binding and dissociation rate constants (k(on) and ko(off)) are extremely high in comparison with those of hemoglobin. The HSA molecule binding eight Fe(II)P molecules can transport about 3.4 mL/dL of oxygen under physiological conditions, corresponding to about 60 % of the oxygen transporting amount of human blood.

UR - http://www.scopus.com/inward/record.url?scp=0031193433&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031193433&partnerID=8YFLogxK

U2 - 10.1021/bc9700906

DO - 10.1021/bc9700906

M3 - Article

C2 - 9258452

AN - SCOPUS:0031193433

VL - 8

SP - 534

EP - 538

JO - Bioconjugate Chemistry

JF - Bioconjugate Chemistry

SN - 1043-1802

IS - 4

ER -