Peroxidase Activity of a c‐Type Cytochrome b5 in the Non‐Native State is Comparable to that of Native Peroxidases

Hu, Shan; He, Bo; Du, Ke; Wang, Xiaojuan; Gao, Shu‐Qin; Lin, Ying‐Wu

doi:10.1002/open.201700055

Cited by 10 publications

(2 citation statements)

References 51 publications

(38 reference statements)

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“…Moreover, both Th 4+ and UO 2 2+ ions reduce the oxy-form of Hb at a high concentration of >100 µM [40]. Cyt b 5 is a small membrane binding heme protein, and its heme-binding domain is highly negatively charged by a series of acidic residues, forming an "acidic" cluster [41][42][43]. Spectroscopic study showed that uranyl may bind to the surface of Cyt b 5 with a binding affinity of K D = 10 µM, and molecular modeling study suggested a possible uranyl binding site at surface residues, Glu37 and Glu43 (Figure 2a) [44,45].…”

Section: Binding To Potential Metal-binding Sitesmentioning

confidence: 99%

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%

Uranyl Binding to Proteins and Structural-Functional Impacts

Lin

2020

Biomolecules

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“…4 To increase the protein stability, especially for the heme-binding affinity of heme proteins, a common approach is to construct a covalent heme to protein cross-link, as occurred in natural cytochrome c (Cyt c) and some Cyt P450s. [28][29][30] For example, a Cyt c-like covalent link (Cys-heme cross-link) has been constructed in Cyt b 5 , [31][32][33] Cyt b 562 , 34 ascorbate peroxidase, 35 and myoglobin (Mb). 36 Moreover, other heme-protein cross-links such as Met-Heme, 37 His-Heme, 38 and Tyr-heme, 39,40 can also be designed in articial heme proteins.…”

Section: Introductionmentioning

confidence: 99%