title: Design, synthesis and peroxidase-like activity of 3alpha-helix proteins covalently bound to heme.
abstract: As a model of artificial peroxidase, de novo designed three-alpha-helix proteins, 3alpha-H9 and 3alpha-H12, covalently bound to Fe(III)-mesoporphyrin IX were synthesized and examined for a peroxidase-like activity. The activity was regulated according to the positions of His residues in the proteins, and the His residues played a role in an acid-base catalytic function.
authors.affiliation: Graduate School ot Bioscience and Biotechnology, Tokyo Institute of Technology, Nagatsuta, Yokohama, Japan.
authors.forename: I
authors.initials: I
authors.lastname: Obataya
authors.forename: T
authors.initials: T
authors.lastname: Kotaki
authors.forename: S
authors.initials: S
authors.lastname: Sakamoto
authors.forename: A
authors.initials: A
authors.lastname: Ueno
authors.forename: H
authors.initials: H
authors.lastname: Mihara
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D015195:Drug Design; D006418:Heme / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D018716:Molecular Mimicry; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology; D010544:Peroxidases / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D017433:Protein Structure, Secondary; D013056:Spectrophotometry, Ultraviolet
chemical_list: D010455:Peptides; D006418:Heme; D010544:Peroxidases