Protein metalation in a nutshell

Osman, Deenah; Robinson, Nigel J.

doi:10.1002/1873-3468.14500

Protein metalation in a nutshell

Osman, Deenah; Robinson, Nigel J.

Authors

Deenah Osman

Professor Nigel Robinson nigel.robinson@durham.ac.uk
Professor

Abstract

Metalation, the acquisition of metals by proteins, must avoid mis-metalation with tighter binding metals. This is illustrated by four selected proteins that require different metals: all show similar ranked orders of affinity for bioavailable metals, as described in a universal affinity series (the Irving-Williams series). Crucially, cellular protein metalation occurs in competition with other metal binding sites. The strength of this competition defines the intracellular availability of each metal: its magnitude has been estimated by calibrating a cells’ set of DNA-binding, metal-sensing, transcriptional regulators. This has established that metal availabilities (as free energies for forming metal complexes) are maintained to the inverse of the universal series. The tightest binding metals are least available. With these availabilities correct metalation is achieved.

Citation

Osman, D., & Robinson, N. J. (2023). Protein metalation in a nutshell. FEBS Letters, 597(1), 141-150. https://doi.org/10.1002/1873-3468.14500

Journal Article Type	Article
Acceptance Date	Sep 15, 2022
Online Publication Date	Sep 20, 2022
Publication Date	2023-01
Deposit Date	Sep 21, 2022
Publicly Available Date	Sep 22, 2022
Journal	FEBS Letters
Print ISSN	0014-5793
Electronic ISSN	1873-3468
Publisher	Federation of European Biochemical Societies
Peer Reviewed	Peer Reviewed
Volume	597
Issue	1
Pages	141-150
DOI	https://doi.org/10.1002/1873-3468.14500
Public URL	https://durham-repository.worktribe.com/output/1191449
Additional Information	Special Issue: Visions of bio-inorganic chemistry: Metals and the molecules of life

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© 2022 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.

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