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Updated: Mar 15, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
Published on: July 9, 2015
Reconstitution of Heme Enzymes with Artificial Metalloporphyrinoids
1Department of Applied Chemistry, Graduate School of Engineering, Osaka University, Suita, Japan; Frontier Research Base for Global Young Researchers, Graduate School of Engineering, Osaka University, Suita, Japan; PRESTO, Japan Science and Technology Agency, Kawaguchi, Japan.
Abstract:
An important strategy used in engineering of hemoproteins to generate artificial enzymes involves replacement of heme with an artificial cofactor after removal of the native heme cofactor under acidic conditions. Replacement of heme in an enzyme with a nonnatural metalloporphyrinoid can significantly alter the reactivity of the enzyme. This chapter describes the design and synthesis of three types of artificial metalloporphyrinoid cofactors consisting of mono-, di-, and tri-anionic ligands (tetradehydrocorrin, porphycene, and corrole, respectively). In addition, practical procedures for the preparation of apo-hemoproteins, incorporation of artificial cofactors, and characterization techniques are presented. Furthermore, the representative catalytic activities of artificial enzymes generated by reconstitution of hemoproteins are summarized.
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