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New Active‐Site Analogues of Chloraperoxidase—Syntheses and Catalytic Reactions
Author(s) -
Wagenknecht HansAchim,
Woggon WolfDietrich
Publication year - 1997
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199703901
Subject(s) - chemistry , catalysis , porphyrin , catalytic cycle , heme , active site , stereochemistry , medicinal chemistry , combinatorial chemistry , photochemistry , organic chemistry , enzyme
The iron( III ) porphyrin 1 catalyzes the chlorination of activated CH bonds. It is therefore a model compound for the as yet unidentified intermediate of the catalytic cycle of the heme–thiolate protein chloroperoxidase (CPO). Neither “free HOCl” nor Cl • are involved in the CPO‐catalyzed chlorination, but rather an iron‐bound HOCl is the source of Cl + .
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