448-71-5Relevant articles and documents
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Corwin,Sydow
, p. 4484 (1953)
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McEwen
, p. 711,713 (1946)
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Studies on the tetramerization of substituted monopyrroles to type I porphyrins
Pichon-Santander,Scott
, p. 6967 - 6969 (2007/10/03)
Investigation of the tetramerization of pyrroles bearing two different electron-donating groups as substituents led to the rapid preparation under slightly acidic conditions of a porphyrin analog family with a high ratio of type I isomer for enzymatic act
Syntheses of type-I porphyrins via monopyrrole tetramerization
Nguyen, Liem T.,Smith, Kevin M.
, p. 7177 - 7180 (2007/10/03)
Treatment of 2-[(N,N-dialkylamino)methyl]pyrrole-5-carboxylic acids (e.g. 10,12 or 11,13) in methanol with K3Fe(CN)6 gives type-I porphyrins (etioporphyrin-I 7, coproporphyrin-I tetramethyl ester 16, respectively); with pyrroles 10,12 the product 7 is contaminated with about 8% of other type-isomer(s).
Syntheses and catalytic activities of new cytochrome P-450 model compounds. Effect of peptide chains
Ohkatsu,Watanabe,Goto,Wakita
, p. 742 - 747 (2007/10/02)
As cytochrome P-450 model compounds with structures similar to heme proteins, we designed and synthesized novel porphyrin iron (III) chloride complexes, 11 and 12, which have three peptide chains (3PCs) and four peptide chains (4PCs), and evaluated their catalytic activities. The asymmetric porphyrin complexes are derived from etioporphyrin and peptide chains equivalent to proteins were provided by ring-opening polymerization of N-carboxy L-amino acid anhydride (L-Phe-NCA, γ-BLG-NCA, and N(ε)-benzyloxycarbonyl-L-Lys-NCA) initiated by amino groups on meso positions. The new asymmetric porphyrin complex, 11 or 12, was used for asymmetric epoxidations of styrene as is done by cytochrome P-450. The iron complex achieved the induction of asymmetry, although it has no special conformation, and gave S-styrene oxide in excess (ca. 60%ee). It was found, furthermore, that asymmetric induction was affected by the kind of amino acid residue, the number of peptide chains, and length of peptide chains.