Metal fluorides as analogues for studies on phosphoryl transfer enzymes

Jin, Yi ORCID: https://orcid.org/0000-0002-6927-4371, Richards, Nigel G. J. ORCID: https://orcid.org/0000-0002-0375-0881, Waltho, Jonathan P. and Blackburn, G. Michael 2017. Metal fluorides as analogues for studies on phosphoryl transfer enzymes. Angewandte Chemie - International Edition 56 (15) , pp. 4110-4128. 10.1002/anie.201606474

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Abstract

The 1994 structure of a transition-state analogue with AlF4− and GDP complexed to G1α, a small G protein, heralded a new field of research into the structure and mechanism of enzymes that manipulate the transfer of phosphoryl (PO3−) groups. The number of enzyme structures in the PDB containing metal fluorides (MFx) as ligands that imitate either a phosphoryl or a phosphate group was 357 at the end of 2016. They fall into three distinct geometrical classes: 1) Tetrahedral complexes based on BeF3− that mimic ground-state phosphates; 2) octahedral complexes, primarily based on AlF4−, which mimic “in-line” anionic transition states for phosphoryl transfer; and 3) trigonal bipyramidal complexes, represented by MgF3− and putative AlF30 moieties, which mimic the geometry of the transition state. The interpretation of these structures provides a deeper mechanistic understanding into the behavior and manipulation of phosphate monoesters in molecular biology. This Review provides a comprehensive overview of these structures, their uses, and their computational development.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Chemistry
Subjects:	Q Science > QD Chemistry
Uncontrolled Keywords:	19F NMR spectroscopy; enzyme mechanisms; metal fluorides; phosphoryl transfer; transition-state analogues
Publisher:	Wiley-Blackwell
ISSN:	1433-7851
Date of First Compliant Deposit:	10 April 2017
Date of Acceptance:	21 March 2017
Last Modified:	06 Jan 2024 02:24
URI:	https://orca.cardiff.ac.uk/id/eprint/99784

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