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BN/CC Isosteric Compounds as Enzyme Inhibitors: N ‐ and B ‐Ethyl‐1,2‐azaborine Inhibit Ethylbenzene Hydroxylation as Nonconvertible Substrate Analogues
Author(s) -
Knack Daniel H.,
Marshall Jonathan L.,
Harlow Gregory P.,
Dudzik Agnieszka,
Szaleniec Maciej,
Liu ShihYuan,
Heider Johann
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201208351
Subject(s) - ethylbenzene , chemistry , substrate (aquarium) , reactivity (psychology) , hydroxylation , enzyme , stereochemistry , organic chemistry , toluene , biology , medicine , ecology , alternative medicine , pathology
Good substrate gone bad! BN/CC isosterism of ethylbenzene leads to N ‐ethyl‐1,2‐azaborine and B ‐ethyl‐1,2‐azaborine. In contrast to ethylbenzene, which is the substrate for ethylbenzene dehydrogenase (EbDH), N ‐ethyl‐1,2‐azaborine (see scheme; Fc=Ferricenium tetrafluoroborate) and B ‐ethyl‐1,2‐azaborine are strong inhibitors of EbDH. Thus, the changes provided by BN/CC isosterism can lead to new biochemical reactivity.