Premium
Electrochemically and Catalytically Active Reconstituted Horseradish Peroxidase with Ferrocene‐Modified Hemin and an Artificial Binding Site
Author(s) -
Ryabov Alexander D.,
Goral Vasily N.,
Gorton Lo,
Csöregi Elisabeth
Publication year - 1999
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/(sici)1521-3765(19990301)5:3<961::aid-chem961>3.0.co;2-c
Subject(s) - horseradish peroxidase , hemin , chemistry , ferrocene , peroxidase , combinatorial chemistry , abts , active site , enzyme , polymer chemistry , organic chemistry , heme , electrochemistry , electrode , antioxidant , dpph
The cofactor hemin modified with aminomethylferrocene was loaded into the apo form of horseradish peroxidase (HRP) to give Fc‐HRP (scheme); this reconstituted enzyme is electrochemically and catalytically active with respect to ABTS and water‐soluble ferrocenes. The ferrocenes display kinetically meaningful affinity to the reconstituted enzyme owing to creation of a novel artificial hydrophobic binding site at the protein surface.