BN/CC Isosteric Compounds as Enzyme Inhibitors:  N ‐ and  B ‐Ethyl‐1,2‐azaborine Inhibit Ethylbenzene Hydroxylation as Nonconvertible Substrate Analogues | Zendy

Knack Daniel H. | Zendy; Marshall Jonathan L. | Zendy; Harlow Gregory P. | Zendy; Dudzik Agnieszka | Zendy; Szaleniec Maciej | Zendy; Liu ShihYuan | Zendy; Heider Johann | Zendy

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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.

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