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Bacterial sensors define intracellular free energies for correct enzyme metalation

Osman, Deenah; Martini, Maria Alessandra; Foster, Andrew W.; Chen, Junjun; Scott, Andrew J.P.; Morton, Richard J.; Steed, Jonathan W.; Lurie-Luke, Elena; Huggins, Thomas G.; Lawrence, Andrew D.; Deery, Evelyne; Warren, Martin J.; Chivers, Peter T.; Robinson, Nigel J.

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Authors

Deenah Osman

Maria Alessandra Martini

Andrew W. Foster

Junjun Chen

Andrew J.P. Scott

Richard J. Morton

Elena Lurie-Luke

Thomas G. Huggins

Andrew D. Lawrence

Evelyne Deery

Martin J. Warren



Abstract

There is a challenge for metalloenzymes to acquire their correct metals because some inorganic elements form more stable complexes with proteins than do others. These preferences can be overcome provided some metals are more available than others. However, while the total amount of cellular metal can be readily measured, the available levels of each metal have been more difficult to define. Metal-sensing transcriptional regulators are tuned to the intracellular availabilities of their cognate ions. Here we have determined the standard free energy for metal complex formation to which each sensor, in a set of bacterial metal sensors, is attuned: the less competitive the metal, the less favorable the free energy and hence the greater availability to which the cognate allosteric mechanism is tuned. Comparing these free energies with values derived from the metal affinities of a metalloprotein reveals the mechanism of correct metalation exemplified here by a cobalt chelatase for vitamin B12.

Citation

Osman, D., Martini, M. A., Foster, A. W., Chen, J., Scott, A. J., Morton, R. J., …Robinson, N. J. (2019). Bacterial sensors define intracellular free energies for correct enzyme metalation. Nature Chemical Biology, 15(3), 241-249. https://doi.org/10.1038/s41589-018-0211-4

Journal Article Type Article
Acceptance Date Dec 4, 2018
Online Publication Date Jan 28, 2019
Publication Date Mar 31, 2019
Deposit Date Nov 21, 2018
Publicly Available Date Jul 28, 2019
Journal Nature Chemical Biology
Print ISSN 1552-4450
Electronic ISSN 1552-4469
Publisher Nature Research
Peer Reviewed Peer Reviewed
Volume 15
Issue 3
Pages 241-249
DOI https://doi.org/10.1038/s41589-018-0211-4
Public URL https://durham-repository.worktribe.com/output/1313312
Publisher URL https://rdcu.be/biPEi

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