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Enantioselectivity in Enzyme‐Catalyzed Electron Transfer to and from Planar Chiral Organometallic Compounds
Author(s) -
Ryabov Alexander D.,
Firsova Yulia N.,
Goral Vasily N.,
Ryabova Ekaterina S.,
Shevelkova Angeli.,
Troitskaya Ludmila L.,
Demeschik Tatyana V.,
Sokolov Viatcheslav I.
Publication year - 1998
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(19980515)4:5<806::aid-chem806>3.0.co;2-b
Subject(s) - horseradish peroxidase , enantioselective synthesis , chirality (physics) , chemistry , catalysis , electron transfer , peroxidase , planar chirality , axial chirality , glucose oxidase , planar , enzyme , oxidase test , combinatorial chemistry , stereochemistry , photochemistry , organic chemistry , chiral symmetry , physics , quantum mechanics , nambu–jona lasinio model , computer graphics (images) , computer science , quark
Unnatural substrates (ferrocenes) with unnatural chirality type (planar chirality) are kinetically recognized by horseradish peroxidase (HRP), but not by chloroperoxidase (CLP), in one‐electron HRP‐ and CLP‐catalyzed oxidation of ( S )‐ and ( R )‐2‐methylferrocene carboxylic acid ( 1 , right) into the corresponding ferricenium cations. The enzymatic reduction of ( S )‐ 1 + and ( R )‐ 1 + by reduced glucose oxidase (GO) is also enantioselective.