Biogenic manganese oxide nanoparticle formation by a multimeric multicopper oxidase Mnx

Romano, Christine A.; Zhou, Mowei; Song, Yang; Wysocki, Vicki H.; Dohnálková, Alice; Kovařík, Libor; Paša‐Tolić, Ljiljana; Tebo, Bradley M.

doi:10.1038/s41467-017-00896-8

Cited by 78 publications

(89 citation statements)

References 66 publications

(73 reference statements)

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“…It is then desirable to develop facile, cheap, environmentally benign, and size control routes to prepare MnO2 nanoparticles [34]. In particular, biogenic approaches for the preparation of nanomaterials can be a good alternative to achieve the advantages mentioned above [35]. Non-hazardous chemicals, biodegradable polymers, available fruits, vegetables, herbs containing high concentration of polyphenols can act as antioxidants or reducing agents and can also provide a protective coating.…”

Section: Introductionmentioning

confidence: 99%

Electrochemical performance of nanosized MnO2 synthesized by redox route using biological reducing agents

Abuzeid

Hashem

Kaus

et al. 2018

Journal of Alloys and Compounds

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For more than a century, manganese dioxides (MDOs) have been used as electrochemically active materials in energy storage and conversion applications. To reduce the cost and hazardous impact of synthesis, a redox method was used to prepare MnO2 using extracts of green (GT-MnO2) and black (BT-MnO2) tea as biological reducing agents. Polyphenols present in the extracts of tea not only reduce Mn 7+ ions but also act as "capping agents" to stabilize and prevent the produced MnO2 nanoparticles from degradation and aggregation. Elemental, structural properties and morphology of nanosized α-KxMnO2 were studied by thermogravimetric analysis, X-ray powder diffraction and Raman spectroscopy, which revealed the different crystallinity between GT-MnO2 and BT-MnO2 due to the strength of the antioxidant species. Electrochemical investigations highlight the beneficial presence of K + ions in (2×2) tunnels; with a higher concentration, α-K0.135MnO2 exhibits a discharge specific capacity of 155 mAh g-1 after 20 cycles at C/26 rate.

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Section: Introductionmentioning

confidence: 99%

Electrochemical performance of nanosized MnO2 synthesized by redox route using biological reducing agents

Abuzeid

Hashem

Kaus

et al. 2018

Journal of Alloys and Compounds

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“…We have previously shown that SID produces fragments in which the charge is more symmetrically partitioned than it is in CID and that products can remain compact (13)(14)(15). In addition, we have demonstrated that SID disassembly pathways are consistent with the known protein assembly pathways and hence can provide structural information on known and unknown structures (16)(17)(18). To expand upon…”

mentioning

confidence: 99%

Relative interfacial cleavage energetics of protein complexes revealed by surface collisions

Harvey

Seffernick

Quintyn

et al. 2019

Proc. Natl. Acad. Sci. U.S.A.

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132

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To fulfill their biological functions, proteins must interact with their specific binding partners and often function as large assemblies composed of multiple proteins or proteins plus other biomolecules. Structural characterization of these complexes, including identification of all binding partners, their relative binding affinities, and complex topology, is integral for understanding function. Understanding how proteins assemble and how subunits in a complex interact is a cornerstone of structural biology. Here we report a native mass spectrometry (MS)-based method to characterize subunit interactions in globular protein complexes. We demonstrate that dissociation of protein complexes by surface collisions, at the lower end of the typical surface-induced dissociation (SID) collision energy range, consistently cleaves the weakest protein:protein interfaces, producing products that are reflective of the known structure. We present here combined results for multiple complexes as a training set, two validation cases, and four computational models. We show that SID appearance energies can be predicted from structures via a computationally derived expression containing three terms (number of residues in a given interface, unsatisfied hydrogen bonds, and a rigidity factor).protein complex | native mass spectrometry | protein interactions | structural biology | surface-induced dissociation N ative mass spectrometry (MS) has emerged as a powerful structural biology tool. By using "soft" ionization techniques such as nanoelectrospray ionization, noncovalent interactions can be retained, enabling the study of intact protein:protein, protein: ligand, and protein:RNA complexes in the gas phase (1-4). Native MS overcomes many of the barriers associated with traditional protein characterization methods; it requires low sample volumes (3-10 μL) and micromolar or lower concentrations, while also having a broad mass range for analysis, allowing study of small monomeric proteins up to large megadalton assemblies (1,5).Typical MS experiments to study subunit interactions of protein complexes involve first preparing the sample in an aqueous solution at near neutral pH, typically 100-200 mM ammonium acetate. The complex is then introduced intact into the mass spectrometer to measure the mass of the native complex. To obtain subunit connectivity information on the sample, the complex can be disrupted in solution, typically either with small volumes of organic solvent or through alteration of the ionic strength; this destabilizes the protein:protein interfaces and allows measurement of stable subcomplexes (6, 7). This approach, however, targets all species present in solution and can therefore be problematic for heterogeneous samples where it may not be possible to decipher which subcomplex came from which precursor. Alternatively, the complex can be isolated and then dissociated in the gas phase. The most commonly used dissociation method for such studies is collision-induced dissociation (CID). In CID protein ions are accelerated i...

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“…In this technique, protein complexes are dissociated by collision with a surface. The SID products of a complex are often sufficient to gain insight into the complex architecture (26,27). SID was performed by directing and accelerating the protein complex ions to an off-axis surface.…”

Section: Resultsmentioning

confidence: 99%

“…Additionally, ion mobility (IM) measurements can be used to also determine their collision cross-sections (CCSs) in a combined IM-MS approach. These IM-MS measurements provide information on the stoichiometry and shape of the intact protein complex in the gas phase (24)(25)(26)(27). The protein complex ion of a particular charge state can be selected by a quadrupole and subjected to surface-induced dissociation (SID) before IM-MS. SID is a single-step, high-energy activation method, wherein noncovalent dissociation of the complex leads to generation of Significance Recent advancements in computational protein design have enabled the generation of proteins and protein complexes that are not present in nature.…”

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confidence: 99%

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Confirmation of intersubunit connectivity and topology of designed protein complexes by native MS

Sahasrabuddhe

Hsia

Büsch

et al. 2018

Proc. Natl. Acad. Sci. U.S.A.

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Computational protein design provides the tools to expand the diversity of protein complexes beyond those found in nature. Understanding the rules that drive proteins to interact with each other enables the design of protein-protein interactions to generate specific protein assemblies. In this work, we designed protein-protein interfaces between dimers and trimers to generate dodecameric protein assemblies with dihedral point group symmetry. We subsequently analyzed the designed protein complexes by native MS. We show that the use of ion mobility MS in combination with surface-induced dissociation (SID) allows for the rapid determination of the stoichiometry and topology of designed complexes. The information collected along with the speed of data acquisition and processing make SID ion mobility MS well-suited to determine key structural features of designed protein complexes, thereby circumventing the requirement for more time- and sample-consuming structural biology approaches.

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Biogenic manganese oxide nanoparticle formation by a multimeric multicopper oxidase Mnx

Cited by 78 publications

References 66 publications

Electrochemical performance of nanosized MnO2 synthesized by redox route using biological reducing agents

Electrochemical performance of nanosized MnO2 synthesized by redox route using biological reducing agents

Relative interfacial cleavage energetics of protein complexes revealed by surface collisions

Confirmation of intersubunit connectivity and topology of designed protein complexes by native MS

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