19F NMR studies on γ-butyrobetaine hydroxylase provide mechanistic insights and suggest a dual inhibition mode. Issue 98 (8th November 2019)

• Record Type: Journal Article
• Authors: Leśniak, Robert K.; Rydzik, Anna M.; Kamps, Jos J. A. G.; Kahn, Amjad; Claridge, Timothy D. W.; Schofield, Christopher J.
• Is Part Of: Chemical communications. Volume 55:Issue 98(2019)
• Page Start: 14717
• Page End: 14720
• Publication Date: 2019-11-08
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c9cc06466d
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : 19 F and 1 H NMR studies on fluorine labelled γ-butyrobetaine hydroxylase provide mechanistic insight into substrate and ligand binding, suggesting cooperativity between two monomers. Abstract : The final step in the biosynthesis of l -carnitine in humans is catalysed by the 2-oxoglutarate and ferrous iron dependent oxygenase, γ-butyrobetaine hydroxylase (BBOX). 1 H and 19 F NMR studies inform on the BBOX mechanism including by providing evidence for cooperativity between monomers in substrate/some inhibitor binding. The value of the 19 F NMR methods is demonstrated by their use in the design of new BBOX inhibitors.