Iron porphyrin-cyclodextrin supramolecular complex as a functional model of myoglobin in aqueous solution

Koji Kano, Hiroaki Kitagishi, Camille Dagallier, Masahito Kodera, Takashi Matsuo, Takashi Hayashi, Yoshio Hisaeda, Shun Hirota

Research output: Contribution to journalArticle

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Abstract

The 1:1 inclusion complex of 5,10,15,20-tetrakis(4-sulfonatophenyl) porphinato iron(II) (FeIITPPS) and an O-methylated β-cyclodextrin dimer having a pyridine linker (1) binds dioxygen reversibly in aqueous solution. The O2 adduct was very stable (t1/2 = 30.1 h) at pH 7.0 and 25°C. ESI-MS and NMR spectroscopic measurements and molecular mechanics (MM) calculations indicated the inclusion of the sulfonatophenyl groups at the 5- and 15-positions of FeIIITPPS or FeIITPPS into two cyclodextrin moieties of 1, to form a supramolecular 1:1 complex (hemoCD1 for the FeIITPPS complex), whose iron center is completely covered by two cyclodextrin moieties. Equilibrium measurements and laser flash photolysis provided the affinities (P 1/2O2 and P1/2CO) and rate constants for O2 and CO binding of hemoCD1 (konO2, koffO2, konCO, and k offCO). The CO affinity relative to the O2 affinity of hemoCD1 was abnormally high. Although resonance Raman spectra suggested weak back-bonding of dπ(Fe) → π*(CO) and hence a weak CO-Fe bond, the CO adduct of hemoCD1 was very stable. The hydrophobic CO molecule dissociated from CO-hemoCD1 hardly breaks free from a shallow cleft in hemoCD1 surrounded by an aqueous bulk phase leading to fast rebinding of CO to hemoCD1. Isothermal titration calorimetry furnished the association constant (KO2), ΔH°, and ΔS° for O2 association to be (2.71 ± 0.51) × 104 M-1, -65.2 ± 4.4 kJ mol-1, and -133.9 ± 16.1 J mol-1 K-1, respectively. The autoxidation of oxy-hemoCD1 was accelerated by H+ and OH-. The inorganic anions also accelerated the autoxidation of oxy-hemoCD1. The O 2-FeII bond is equivalent to the O2 •--FeIII bond, which is attacked by the inorganic anions or the water molecule to produce met-hemoCD1 and a superoxide anion.

Original languageEnglish
Pages (from-to)4448-4460
Number of pages13
JournalInorganic chemistry
Volume45
Issue number11
DOIs
Publication statusPublished - May 29 2006

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myoglobin
Myoglobin
Porphyrins
Cyclodextrins
Carbon Monoxide
porphyrins
affinity
Iron
anions
aqueous solutions
iron
adducts
inclusions
inorganic peroxides
titration
flash
photolysis
molecules
pyridines
heat measurement

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry

Cite this

Kano, K., Kitagishi, H., Dagallier, C., Kodera, M., Matsuo, T., Hayashi, T., ... Hirota, S. (2006). Iron porphyrin-cyclodextrin supramolecular complex as a functional model of myoglobin in aqueous solution. Inorganic chemistry, 45(11), 4448-4460. https://doi.org/10.1021/ic060137b

Iron porphyrin-cyclodextrin supramolecular complex as a functional model of myoglobin in aqueous solution. / Kano, Koji; Kitagishi, Hiroaki; Dagallier, Camille; Kodera, Masahito; Matsuo, Takashi; Hayashi, Takashi; Hisaeda, Yoshio; Hirota, Shun.

In: Inorganic chemistry, Vol. 45, No. 11, 29.05.2006, p. 4448-4460.

Research output: Contribution to journalArticle

Kano, K, Kitagishi, H, Dagallier, C, Kodera, M, Matsuo, T, Hayashi, T, Hisaeda, Y & Hirota, S 2006, 'Iron porphyrin-cyclodextrin supramolecular complex as a functional model of myoglobin in aqueous solution', Inorganic chemistry, vol. 45, no. 11, pp. 4448-4460. https://doi.org/10.1021/ic060137b
Kano K, Kitagishi H, Dagallier C, Kodera M, Matsuo T, Hayashi T et al. Iron porphyrin-cyclodextrin supramolecular complex as a functional model of myoglobin in aqueous solution. Inorganic chemistry. 2006 May 29;45(11):4448-4460. https://doi.org/10.1021/ic060137b
Kano, Koji ; Kitagishi, Hiroaki ; Dagallier, Camille ; Kodera, Masahito ; Matsuo, Takashi ; Hayashi, Takashi ; Hisaeda, Yoshio ; Hirota, Shun. / Iron porphyrin-cyclodextrin supramolecular complex as a functional model of myoglobin in aqueous solution. In: Inorganic chemistry. 2006 ; Vol. 45, No. 11. pp. 4448-4460.
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