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Human Serum Albumin‐Based Peroxidase Having an Iron Protoporphyrin IX in Artificial Heme Pocket
Author(s) -
Watanabe Kyohei,
Ishikawa Natsuki,
Komatsu Teruyuki
Publication year - 2012
Publication title -
chemistry – an asian journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.18
H-Index - 106
eISSN - 1861-471X
pISSN - 1861-4728
DOI - 10.1002/asia.201200373
Subject(s) - heme , peroxidase , protoporphyrin ix , guaiacol , human serum albumin , chemistry , biochemistry , protoporphyrin , mutant , hemeprotein , recombinant dna , enzyme , gene , organic chemistry , porphyrin , photodynamic therapy
Cooking up enzymes : Iron protoporphyrin IX (heme) is bound within a hydrophobic cavity in subdomain IB of human serum albumin (HSA). Site‐specific mutations to introduce proximal and distal histidines into the heme pocket of HSA conferred a peroxidase activity to the prosthetic heme group. The catalytic activity of the recombinant HSA(mutant)–heme complex for guaiacol oxidation is 17‐fold higher than that of HSA(wild type)–heme.