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- Title
New Enzyme Models of Chloroperoxidase: Improved stability and catalytic efficiency of iron porphyrinates containing a thiolato ligand.
- Authors
Wagenknecht, Hans-Achim; Claude, Cécile; Woggon, Wolf-Dietrich
- Abstract
The heme-thiolate protein chloroperoxidase (CPO) catalyzes the chlorination of activated CH bonds. A reaction mechanism is proposed for this enzymatic transformation ( Scheme 1), and a new iron(III) porphyrinate complex 13 is synthesized containing pentafluorophenyl groups at two meso-positions and a thiophenolato ligand coordinating to the Fe-atom ( Schemes 2 and 3). Due to the presence of the electron-withdrawing substituents, the catalyst 13 is appreciably resistant to oxidants (HOCl) and chlorinates, e.g., monochlorodimedone ( 5), with turnover numbers up to 1530. The redox potential of 13, E0 = - 134 mV, and the Soret band (λmax 448 nm) of the CO adduct of the reduced state of 13 are close to the corresponding values of the enzyme CPO.
- Publication
Helvetica Chimica Acta, 1998, Vol 81, Issue 5-8, p1506
- ISSN
0018-019X
- Publication type
Article
- DOI
10.1002/hlca.19980810554