BN/CC Isosteric Compounds as Enzyme Inhibitors: N‐ and B‐Ethyl‐1, 2‐azaborine Inhibit Ethylbenzene Hydroxylation as Nonconvertible Substrate Analogues1. Issue 9 (28th January 2013)

• Record Type: Journal Article
• Authors: Knack, Daniel H.; Marshall, Jonathan L.; Harlow, Gregory P.; Dudzik, Agnieszka; Szaleniec, Maciej; Liu, Shih‐Yuan; Heider, Johann
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 9(2013)
• Page Start: 2599
• Page End: 2601
• Publication Date: 2013-01-28
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201208351
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Good substrate gone bad!</bold> BN/CC isosterism of ethylbenzene leads to <italic>N</italic>‐ethyl‐1, 2‐azaborine and <italic>B</italic>‐ethyl‐1, 2‐azaborine. In contrast to ethylbenzene, which is the substrate for ethylbenzene dehydrogenase (EbDH), <italic>N</italic>‐ethyl‐1, 2‐azaborine (see scheme; Fc=Ferricenium tetrafluoroborate) and <italic>B</italic>‐ethyl‐1, 2‐azaborine are strong inhibitors of EbDH. Thus, the changes provided by BN/CC isosterism can lead to new biochemical reactivity.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1v49fmhc" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>