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Cover Picture: A Myoglobin Functional Model Composed of a Ferrous Porphyrin and a Cyclodextrin Dimer with an Imidazole Linker (Chem. Asian J. 3/2006)
Author(s) -
Kano Koji,
Kitagishi Hiroaki,
Mabuchi Takahiro,
Kodera Masahito,
Hirota Shun
Publication year - 2006
Publication title -
chemistry – an asian journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.18
H-Index - 106
eISSN - 1861-471X
pISSN - 1861-4728
DOI - 10.1002/asia.200690003
Subject(s) - porphyrin , chemistry , myoglobin , linker , imidazole , dimer , pyrazine , carbon monoxide , aqueous solution , cyclodextrin , ferrous , pyridine , photochemistry , crystallography , stereochemistry , medicinal chemistry , organic chemistry , catalysis , computer science , operating system
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.