Human serum albumin-based peroxidase having an iron protoporphyrin IX in artificial heme pocket.
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.
Department of Applied Chemistry, Faculty of Science and Engineering, Chuo University, 1-13-27 Kasuga, Bunkyo-ku, Tokyo 112-8551, Japan.
Kyohei
K
Watanabe
Natsuki
N
Ishikawa
Teruyuki
T
Komatsu
D006139:Guaiacol / Q000737:chemistry; D006418:Heme / Q000737:chemistry*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D016297:Mutagenesis, Site-Directed; D010084:Oxidation-Reduction; D009195:Peroxidase / Q000737:chemistry / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011524:Protoporphyrins / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012709:Serum Albumin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D011524:Protoporphyrins; D011994:Recombinant Proteins; D012709:Serum Albumin; C448299:iron protoporphyrin IX; D006418:Heme; D006139:Guaiacol; D009195:Peroxidase