Cover Picture: A Myoglobin Functional Model Composed of a Ferrous Porphyrin and a Cyclodextrin Dimer with an Imidazole Linker (Chem. Asian J. 3/2006)

Science imitates life in a 1:1 inclusion complex (Fe II PorImCD) of 5,10,15,20‐tetrakis(4‐sulfonatophenyl)porphinatoiron(II) (Fe II Por) and an O‐methylated β‐cyclodextrin (ImCD) dimer with an imidazole linker. This complex was found to mimic myoglobin and bind dioxygen and carbon monoxide in aqueou...

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Veröffentlicht in:Chemistry, an Asian journal an Asian journal, 2006-09, Vol.1 (3), p.295-295
Hauptverfasser: Kano, Koji, Kitagishi, Hiroaki, Mabuchi, Takahiro, Kodera, Masahito, Hirota, Shun
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Sprache:eng
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Zusammenfassung:Science imitates life in a 1:1 inclusion complex (Fe II PorImCD) of 5,10,15,20‐tetrakis(4‐sulfonatophenyl)porphinatoiron(II) (Fe II Por) and an O‐methylated β‐cyclodextrin (ImCD) dimer with an imidazole linker. This complex was found to mimic myoglobin and bind dioxygen and carbon monoxide in aqueous solution. The cover picture shows the image of O 2 bound to Fe II PorImCD (the original structure was obtained by MM2 calculations). Fe II PorImCD shows a higher affinity for dioxygen than hemoCD, an analogue with a pyridine axial ligand, but poorer selectivity for carbon monoxide. For more information, see the Full Paper “A Myoglobin Functional Model Composed of a Ferrous Porphyrin and a Cyclodextrin Dimer with an Imidazole Linker” by K. Kano and co‐workers on page 358 ff.
ISSN:1861-4728
1861-471X
DOI:10.1002/asia.200690003