Abstract
Synthetic hemoprotein model compounds are of great interest due to the vital roles and complexities of hemoproteins. This study reports a novel, self-assembled hemoprotein model, hemodextrin. The synthesis and characterization of py-PPCD (2A-monopyridylmethyl-perPEGylated-β -cyclodextrin) (2) is described. The molecular design is based on a pegylated cyclodextrin scaffold that bears both a heme-binding pocket and an axial ligand that binds an iron porphyrin. The binding constant for Fe(III)TPPS [iron(III) meso-tetra(4-sulphonatophenyl)porphyrin] by py-PPCD (2) was determined to be 2×106 M-1 at pH 6.0 by observing characteristic changes in the UV-Vis spectrum of the porphyrin. The pyridyl nitrogen of py-PPCD (2) was shown to ligate to the iron center by observing signal changes in the Fe(II)-porphyrin 1H-NMR spectrum. This hemodextrin ensemble was shown to bind dioxygen reversibly and to form a stable ferryl species.
Original language | English (US) |
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Pages (from-to) | 639-648 |
Number of pages | 10 |
Journal | Biophysical Chemistry |
Volume | 105 |
Issue number | 2-3 |
DOIs | |
State | Published - Sep 1 2003 |
All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Organic Chemistry
Keywords
- Cyclodextrin
- Hemoprotein
- Porphyrin
- Self-assembly