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Open AccessReview

Cellular Dynamics of Transition Metal Exchange on Proteins: A Challenge but a Bonanza for Coordination Chemistry

by 1,2,3
1
Alternative Energies and Atomic Energy Commission—Fundamental Research Division—Interdisciplinary Research Institute of Grenoble (CEA-IRIG), University of Grenoble Alpes, F-38000 Grenoble, France
2
National Institute of Health and Medical Research, University of Grenoble Alpes, Inserm U1055, F-38000 Grenoble, France
3
Laboratory of Fundamental and Applied Bioenergetics (LBFA), University of Grenoble Alpes, Inserm U1055, F-38000 Grenoble, France
Biomolecules 2020, 10(11), 1584; https://doi.org/10.3390/biom10111584
Received: 28 September 2020 / Revised: 16 November 2020 / Accepted: 19 November 2020 / Published: 21 November 2020
(This article belongs to the Special Issue Metal Binding Proteins 2020)
Transition metals interact with a large proportion of the proteome in all forms of life, and they play mandatory and irreplaceable roles. The dynamics of ligand binding to ions of transition metals falls within the realm of Coordination Chemistry, and it provides the basic principles controlling traffic, regulation, and use of metals in cells. Yet, the cellular environment stands out against the conditions prevailing in the test tube when studying metal ions and their interactions with various ligands. Indeed, the complex and often changing cellular environment stimulates fast metal–ligand exchange that mostly escapes presently available probing methods. Reducing the complexity of the problem with purified proteins or in model organisms, although useful, is not free from pitfalls and misleading results. These problems arise mainly from the absence of the biosynthetic machinery and accessory proteins or chaperones dealing with metal / metal groups in cells. Even cells struggle with metal selectivity, as they do not have a metal-directed quality control system for metalloproteins, and serendipitous metal binding is probably not exceptional. The issue of metal exchange in biology is reviewed with particular reference to iron and illustrating examples in patho-physiology, regulation, nutrition, and toxicity. View Full-Text
Keywords: transition metals; redox activity; regulation; chaperone; metal toxicity; inflammation; specificity; labeling; recombinant technology; iron transition metals; redox activity; regulation; chaperone; metal toxicity; inflammation; specificity; labeling; recombinant technology; iron
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MDPI and ACS Style

Moulis, J.-M. Cellular Dynamics of Transition Metal Exchange on Proteins: A Challenge but a Bonanza for Coordination Chemistry. Biomolecules 2020, 10, 1584. https://doi.org/10.3390/biom10111584

AMA Style

Moulis J-M. Cellular Dynamics of Transition Metal Exchange on Proteins: A Challenge but a Bonanza for Coordination Chemistry. Biomolecules. 2020; 10(11):1584. https://doi.org/10.3390/biom10111584

Chicago/Turabian Style

Moulis, Jean-Marc. 2020. "Cellular Dynamics of Transition Metal Exchange on Proteins: A Challenge but a Bonanza for Coordination Chemistry" Biomolecules 10, no. 11: 1584. https://doi.org/10.3390/biom10111584

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