Octahedral Trifluoromagnesate, an anomalous metal fluoride species, stabilizes the transition state in a biological motor

Ge, Mengyu, Molt, Robert W., Jenkins, Huw T., Blackburn, G. Michael, Jin, Yi ORCID: https://orcid.org/0000-0002-6927-4371 and Antson, Alfred A. 2021. Octahedral Trifluoromagnesate, an anomalous metal fluoride species, stabilizes the transition state in a biological motor. ACS Catalysis 11 , 2769–2773. 10.1021/acscatal.0c04500

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Abstract

Isoelectronic metal fluoride transition state analogue (TSA) complexes, MgF3– and AlF4–, have proven to be immensely useful in understanding mechanisms of biological motors utilizing phosphoryl transfer. Here we report a previously unobserved octahedral TSA complex, MgF3(H2O)−, in a 1.5 Å resolution Zika virus NS3 helicase crystal structure. 19F NMR provided independent validation and also the direct observation of conformational tightening resulting from ssRNA binding in solution. The TSA stabilizes the two conformations of motif V of the helicase that link ATP hydrolysis with mechanical work. DFT analysis further validated the MgF3(H2O)− species, indicating the significance of this TSA for studies of biological motors.

Item Type:	Article
Date Type:	Published Online
Status:	Published
Schools:	Chemistry Cardiff Catalysis Institute (CCI)
Publisher:	American Chemical Society
ISSN:	2155-5435
Date of First Compliant Deposit:	18 February 2021
Date of Acceptance:	28 December 2020
Last Modified:	06 Jan 2024 02:24
URI:	https://orca.cardiff.ac.uk/id/eprint/138643

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