BN/CC isosteric compounds as enzyme inhibitors: N- and B-ethyl-1,2-azaborine inhibit ethylbenzene hydroxylation as nonconvertible substrate analogues.
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.
Laboratory for Microbial Biochemistry, Philipps University of Marburg, 35043 Marburg, Germany.
Daniel H
DH
Knack
Jonathan L
JL
Marshall
Gregory P
GP
Harlow
Agnieszka
A
Dudzik
Maciej
M
Szaleniec
Shih-Yuan
SY
Liu
Johann
J
Heider
D001555:Benzene Derivatives / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D001896:Boron Compounds / Q000737:chemistry* / Q000494:pharmacology*; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D006900:Hydroxylation / Q000187:drug effects; D010088:Oxidoreductases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism
C556261:1,2-azaborine; D001555:Benzene Derivatives; D001896:Boron Compounds; D004791:Enzyme Inhibitors; D010088:Oxidoreductases; C121602:ethylbenzene dehydrogenase; C004912:ethylbenzene