Rational Design of Artificial Metalloproteins and Metalloenzymes with Metal Clusters

Lin, Ying‐Wu

doi:10.3390/molecules24152743

Cited by 34 publications

(19 citation statements)

References 133 publications

(181 reference statements)

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“…In addition to a single metal ion or metal cofactor, metalloproteins may harbor multiple metal ions forming metal clusters that play either structural roles, electron-transfer, or catalysis functions [47]. Metallothioneins (MTs) are metalloproteins with metal-clusters and play important roles in both detoxification of heavy metals and scavenge of reactive oxygen species (ROS) [48].…”

Section: Binding To Potential Metal-binding Sitesmentioning

confidence: 99%

“…Acharya and Blindauer reported that UO2 2+ can bind to the cyanobacterial metallothionein SmtA, and form a heterometallic (UO2 2+ )nZn4SmtA species, without alteration of the native Zn4Cys9His2 cluster [49]. 1 H-NMR and molecular modeling studies In addition to a single metal ion or metal cofactor, metalloproteins may harbor multiple metal ions forming metal clusters that play either structural roles, electron-transfer, or catalysis functions [47]. Metallothioneins (MTs) are metalloproteins with metal-clusters and play important roles in both detoxification of heavy metals and scavenge of reactive oxygen species (ROS) [48].…”

Section: Binding To Potential Metal-binding Sitesmentioning

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: Binding To Potential Metal-binding Sitesmentioning

confidence: 99%

Section: Binding To Potential Metal-binding Sitesmentioning

confidence: 99%

Uranyl Binding to Proteins and Structural-Functional Impacts

Lin

2020

Biomolecules

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“…[29] Currently, there is a tremendous interest in the redesign of metal coordination sites. [30,31,32] These centres or clusters can serve as reaction co-factors [33,34], to aid in the electron transfer [35,36], or to serve as scaffolds to carry quantum dots for bio-imaging, sensing or co-catalysis [37,38,39,40,41,22].…”

Section: Introductionmentioning

confidence: 99%

The symmetric designer protein Pizza as a scaffold for metal coordination

et al. 2021

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Symmetric proteins are currently of interest as they allow creation of larger assemblies and facilitate the incorporation of metal ions in the larger complexes. Recently this was demonstrated by the biomineralization of the cadmium-chloride nanocrystal via the Pizza designer protein. However, the mechanism behind this formation remained unclear. Here, we set out to investigate the mechanism driving the formation of this nanocrystal via truncation, mutation, and circular permutations. In addition, the interaction of other biologically relevant metal ions with these symmetric proteins to form larger symmetric complexes was also studied.The formation of the initial nanocrystal is shown to originate from steric strain, where His 58 induces a different rotameric conformation on His 73, thereby distorting an otherwise perfect planar ring of alternating cadmium and chlorine ions, resulting in the smallest nanocrystal.Similar highly symmetric complexes were also observed for the other biological relevant metal ions. However, the flexibility of the coordinating histidine residues allows each metal ion to adopt its preferred geometry leading to either monomeric or dimeric 𝛽𝛽-propeller units, where the metal ions are located at the interface between both propeller units. These results demonstrate that symmetric proteins are not only interesting to generate larger assemblies, but are also the perfect scaffold to create more complex metal based assemblies. Such metal protein assemblies may then find applications in bionanotechnology or biocatalysis.

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“…Although relatively less studied, Mo-clusters have shown promising electrocatalytic activities due to their intermediate behaviors between metal-coordination from comparing structures, properties, and reactivities of metalloenzymes and artificial catalysts [14]. Although relatively less studied, Mo-clusters have shown promising electrocatalytic activities due to their intermediate behaviors between metal-coordination complexes and nanoparticle catalysts [15]. In the perspective of developing efficient electrocatalysts, Mo-nanomaterials, which have shown remarkable electrocatalytic activities, should be considered together.…”

Section: Introductionmentioning

confidence: 99%

Molybdenum-Containing Metalloenzymes and Synthetic Catalysts for Conversion of Small Molecules

2021

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The energy deficiency and environmental problems have motivated researchers to develop energy conversion systems into a sustainable pathway, and the development of catalysts holds the center of the research endeavors. Natural catalysts such as metalloenzymes have maintained energy cycles on Earth, thus proving themselves the optimal catalysts. In the previous research results, the structural and functional analogs of enzymes and nano-sized electrocatalysts have shown promising activities in energy conversion reactions. Mo ion plays essential roles in natural and artificial catalysts, and the unique electrochemical properties render its versatile utilization as an electrocatalyst. In this review paper, we show the current understandings of the Mo-enzyme active sites and the recent advances in the synthesis of Mo-catalysts aiming for high-performing catalysts.

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Rational Design of Artificial Metalloproteins and Metalloenzymes with Metal Clusters

Cited by 34 publications

References 133 publications

Uranyl Binding to Proteins and Structural-Functional Impacts

Uranyl Binding to Proteins and Structural-Functional Impacts

The symmetric designer protein Pizza as a scaffold for metal coordination

Molybdenum-Containing Metalloenzymes and Synthetic Catalysts for Conversion of Small Molecules

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