Frontispiece: Cation–π Interactions Contribute to Substrate Recognition in γ‐Butyrobetaine Hydroxylase Catalysis. Issue 4 (January 2016)

• Record Type: Journal Article
• Authors: Kamps, Jos J. A. G.; Khan, Amjad; Choi, Hwanho; Lesniak, Robert K.; Brem, Jürgen; Rydzik, Anna M.; McDonough, Michael A.; Schofield, Christopher J.; Claridge, Timothy D. W.; Mecinović, Jasmin
• Is Part Of: Chemistry. Volume 22:Issue 4(2016)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2016-01
• Subjects: cation–pi interactions -- C−H oxidation -- enzyme catalysis -- molecular recognition -- oxygenases; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.201680462
• Languages: English
• ISSNs: 0947-6539

Abstract

Abstract : Biocatalysis γ‐Butyrobetaine hydroxylase (BBOX) contains an aromatic cage for the recognition of the positively charged trimethylammonium group of its γ‐butyrobetaine (γBB) substrate. Enyzme binding and kinetic analyses on substrate analogues with P and As substituting for N in the trimethylammonium group show that the analogues are good BBOX substrates, which follow the efficiency trend N + >P + >As +, but an uncharged carbon analogue of γBB is not a good BBOX substrate, thus highlighting the importance of energetically favorable cation–π interactions in productive substrate recognition. For more information, see the Full Paper from J. Mecinović et al. onpage 1270 ff.