Coordination chemistry of f-block metal ions with ligands bearing bio-relevant functional groups

Götzke, Linda; Schaper, Gerrit; März, Juliane; Huittinen, Nina; Stumpf, Thorsten; Kammerlander, Kaitlin Kim Karlotta; Brunner, Eike; Hahn, P. O.; Mehnert, Anne; Kersting, Berthold; Henle, Thomas; Lindoy, Leonard F.; Zanoni, Giuseppe; Weigand, Jan J.

doi:10.1016/j.ccr.2019.01.006

Cited by 43 publications

(26 citation statements)

References 501 publications

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“…Firstly, although plenty of proteins have been discovered to date as the targets of uranyl binding [19], it is still necessary to establish new methods in combination with the advance in computational biology, for probing more potential uranyl-binding sites of native proteins in biological systems.…”

Section: Fetuin-a 3 Binding Sites~30 Nm-10 µMmentioning

confidence: 99%

“…Proteins, especially for metalloproteins, play vital roles in supporting life, including electron-transfer, O2-binding and delivery, and catalysis, etc [11][12][13][14][15][16][17][18]. To date, a plenitude of proteins have been shown to interact with UO2 2+ , such as proteins in blood (human serum albumin, HSA; transferrin, Tf; hemoglobin, Hb), proteins involved in bone growth (osteopontin, OPN; fetuin-A), and the intracellar proteins (metallothionein, MT; cytochromes b5/c; Cyt b5/c; calmodulin, CaM), etc [19]. Although the structural features of some uranyl-protein complexes are well-documented [7][8][9], fewer advances are made in understanding the functional impacts of uranyl-protein interactions, with much less for other actinides-proteins interactions, as reviewed by Creff et al very recently [20].…”

Section: Introductionmentioning

confidence: 99%

“…hemoglobin, Hb), proteins involved in bone growth (osteopontin, OPN; fetuin-A), and the intracellar proteins (metallothionein, MT; cytochromes b 5 /c; Cyt b 5 /c; calmodulin, CaM), etc [19]. Although the structural features of some uranyl-protein complexes are well-documented [7-9], fewer advances are made in understanding the functional impacts of uranyl-protein interactions, with much less for other actinides-proteins interactions, as reviewed by Creff et al very recently [20].…”

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confidence: 99%

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Uranyl Binding to Proteins and Structural-Functional Impacts

Lin

2020

Biomolecules

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The widespread use of uranium for civilian purposes causes a worldwide concern of its threat to human health due to the long-lived radioactivity of uranium and the high toxicity of uranyl ion (UO 2 2+ ). Although uranyl-protein/DNA interactions have been known for decades, fewer advances are made in understanding their structural-functional impacts. Instead of focusing only on the structural information, this article aims to review the recent advances in understanding the binding of uranyl to proteins in either potential, native, or artificial metal-binding sites, and the structural-functional impacts of uranyl-protein interactions, such as inducing conformational changes and disrupting protein-protein/DNA/ligand interactions. Photo-induced protein/DNA cleavages, as well as other impacts, are also highlighted. These advances shed light on the structure-function relationship of proteins, especially for metalloproteins, as impacted by uranyl-protein interactions. It is desired to seek approaches for biological remediation of uranyl ions, and ultimately make a full use of the double-edged sword of uranium.Proteins, especially for metalloproteins, play vital roles in supporting life, including electron-transfer, O 2 -binding and delivery, and catalysis, etc [11][12][13][14][15][16][17][18]. To date, a plenitude of proteins have been shown to interact with UO 2 2+ , such as proteins in blood (human serum albumin, HSA; transferrin, Tf;hemoglobin, Hb), proteins involved in bone growth (osteopontin, OPN; fetuin-A), and the intracellar proteins (metallothionein, MT; cytochromes b 5 /c; Cyt b 5 /c; calmodulin, CaM), etc [19]. Although the structural features of some uranyl-protein complexes are well-documented [7-9], fewer advances are made in understanding the functional impacts of uranyl-protein interactions, with much less for other actinides-proteins interactions, as reviewed by Creff et al. very recently [20]. Instead of focusing only on the structural information, this review highlights the recent advances in understanding the binding of uranyl to proteins, as illustrated in Scheme 1, in either potential, native or artificial metal-binding sites, or the corresponding structural-functional impacts, such as inducing conformational changes and disrupting protein-protein/DNA/ligand interactions. Future directions for studying uranyl-protein interactions are also prospected.

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Section: Fetuin-a 3 Binding Sites~30 Nm-10 µMmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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confidence: 99%

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Uranyl Binding to Proteins and Structural-Functional Impacts

Lin

2020

Biomolecules

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“…Year after year,t he field of inorganic biochemistry is being enriched with discoveries of the biological relevance of lanthanides (Lns) in microorganisms, [1] and their involvement in the methane-cycle and strictly related to the oxidation of methanol and ethanol catalyzed by specificm etal-dependent alcohol dehydrogenases. [2][3][4] In fact the 4f-series of elements( La-Lu) display similar/effective properties to otherc ommonm etals with well-known contribution to physiological and natural processes, such as Ca, Mg and first-row elements such as Fe, Co and Cu, leading to new horizons in biomimetic and de novo systems design, with ab road range of industrial applications. [1,2] Lanthanides have been widely studied and adopted in several fields.…”

Section: Introductionmentioning

confidence: 99%

How Lanthanide Ions Affect the Addition–Elimination Step of Methanol Dehydrogenases

Prejanò

Russo

Marino

2020

Chemistry A European J

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The recently discovered methanol dehydrogenase, XoxF, is a widespread enzyme used by methylotrophic bacteria to oxidize methanol for carbon and energy, and requires lanthanide ions for its activity. This enzyme represents an essential component of methanol utilization by both methanol‐ and methane‐utilizing bacteria. The present investigation looks on the electronic, energetic and geometrical behavior of the methanol dehydrogenase from Methylacidiphilum fumariolicum SolV, which is strictly dependent on early lanthanide metals with +3 oxidation states, by examining enzyme‐substrate complexes of all the lanthanides. We focus on the catalytic reaction mechanism of two methanol dehydrogenases having as cofactor europium and ytterbium belonging to the mid‐ and later‐ series of lanthanides, in comparison with the methanol dehydrogenase containing the cerium, one early lanthanide. Our results provide evidence for the influence of the lanthanide contraction effect in all the elementary steps of the catalytic reaction mechanism. This indication may prove useful for developing new catalytic machineries of enzymes that adopt new‐to‐nature transformations.

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“…Taking inspiration from the Raymond group's use of the hydroxypyridone motif (HOPO, Fig. 1) due to its high affinity for REs in aqueous conditions [39][40][41][42] and potential biomedical applications [43][44][45][46] , we synthesized the novel proligand tris[(1-hydroxy-2-oxo-1,2-dihydropyridine-3-carboxamido)-ethyl]amine, H 3 tren-1,2,3-HOPO·TFA (H 3 1·TFA). We hypothesized that exchanging the positions of the hydroxyl and carbonyl moieties would maintain the high affinity of HOPOderivates for REs while allowing for bridging interactions that were critical for the separations selectivity of our H 3 TriNOx system [35][36][37][38] .…”

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confidence: 99%

High-throughput screening for discovery of benchtop separations systems for selected rare earth elements

et al. 2020

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Rare earth (RE) elements (scandium, yttrium, and the lanthanides) are critical for their role in sustainable energy technologies. Problems with their supply chain have motivated research to improve separations methods to recycle these elements from end of life technology. Toward this goal, we report the synthesis and characterization of the ligand tris[(1-hydroxy-2-oxo-1, 2-dihydropyridine-3-carboxamido)ethyl]amine, H 3 1·TFA (TFA = trifluoroacetic acid), and complexes 1·RE (RE = La, Nd, Dy). A high-throughput experimentation (HTE) screen was developed to quantitatively determine the precipitation of 1·RE as a function of pH as well as equivalents of H 3 1·TFA. This method rapidly determines optimal conditions for the separation of RE mixtures, while minimizing materials consumption. The HTE-predicted conditions are used to achieve the lab-scale separation of Nd/Dy (SF Nd/Dy = 213 ± 34) and La/Nd (SF La/Nd = 16.2 ± 0.2) mixtures in acidic aqueous media.

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Coordination chemistry of f-block metal ions with ligands bearing bio-relevant functional groups

Cited by 43 publications

References 501 publications

Uranyl Binding to Proteins and Structural-Functional Impacts

Uranyl Binding to Proteins and Structural-Functional Impacts

How Lanthanide Ions Affect the Addition–Elimination Step of Methanol Dehydrogenases

High-throughput screening for discovery of benchtop separations systems for selected rare earth elements

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