Nanostructured Carbon Fibres (NCF): Fabrication and Application in Supercapacitor Electrode.

A facile interconnected nanofibre electrode material derived from polybenzimidazol (PBI) was fabricated for a supercapacitor using a centrifugal spinning technique. The PBI solution in a mixture of dimethyl acetamide (DMA) and N, N-dimethylformamide (DMF) was electrospun to an interconnection of fine nanofibres. The as-prepared material was characterised by using various techniques, which include scanning electron microscopy (SEM), X-ray diffractometry (XRD), Raman, X-ray photoelectron spectroscopy (XPS), and Brunauer-Emmett-Teller (BET) among others.

Scientometric trends and knowledge maps of global polychlorinated naphthalenes research over the past four decades.

Polychlorinated naphthalenes (PCNs) were included in the banned list of the Stockholm Convention due to their potential to provoke a wide range of adverse effects on living organisms and the environment. Many reviews have been written to clarify the state of knowledge and identify the research needs of this pollutant class. However, studies have yet to analyse the scientometric complexities of PCN literature.

Advances in the management of radioactive wastes and radionuclide contamination in environmental compartments: a review.

Several anthropogenic activities produce radioactive materials into the environment. According to reports, exposure to high concentrations of radioactive elements such as potassium (K), uranium (U and U), and thorium (Th) poses serious health concerns. The scarcity of reviews addressing the occurrence/sources, distribution, and remedial solutions of radioactive contamination in the ecosystems has fueled data collection for this bibliometric survey.

A bibliometric analysis of pre- and post-Stockholm Convention research publications on the Dirty Dozen Chemicals (DDCs) in the African environment.

Persistent organic pollutants (POPs) are toxic chemicals that stay in the environment for a long time. To address the toxicity issues, global nations, including 53 African countries, ratified the Stockholm Convention to minimize or eliminate the production of 12 POPs known as the "Dirty Dozen". However, these Dirty Dozen Chemicals (DDCs) still exist in significant concentration in the African environment, prompting numerous research to investigate the level of their occurrences.

Bullet-like microstructured nickel ammonium phosphate/graphene foam composite as positive electrode for asymmetric supercapacitors.

Unique microstructured nickel ammonium phosphate Ni(NH)(PO)·4HO and Ni(NH)(PO)·4HO/GF composite were successfully synthesized through the hydrothermal method with different graphene foam (GF) mass loading of 30, 60 and 90 mg as a positive electrode for asymmetric supercapacitors. The crystal structure, vibrational mode, texture and morphology of the samples were studied with X-ray diffraction (XRD), Raman spectroscopy, Brunauer-Emmett-Teller (BET) surface area analysis and scanning electron microscopy (SEM). The prepared materials were tested in both 3-and 2-electrode measurements using 6 M KOH electrolyte.

Electrochemical analysis of Na-Ni bimetallic phosphate electrodes for supercapacitor applications.

Bimetallic sodium-nickel phosphate/graphene foam composite (NaNi(PO)/GF) was successfully synthesized using a direct and simple precipitation method. The hierarchically structured composite material was observed to have demonstrated a synergistic effect between the conductive metallic cations and the graphene foam that made up the composite. The graphene served as a base-material for the growth of NaNi(PO) particles, resulting in highly conductive composite material as compared to the pristine material.

Deciphering the Structural, Textural, and Electrochemical Properties of Activated BN-Doped Spherical Carbons.

In this study, the effect of K₂CO₃ activation on the structural, textural, and electrochemical properties of carbon spheres (CSs) and boron and nitrogen co-doped carbon spheres (BN-CSs) was evaluated. Activation of the CSs and BN-CSs by K₂CO₃ resulted in increased specific surface areas and I/I ratios. From the X-ray photoelectron spectroscopy (XPS) results, the BN-CSs comprised of 64% pyridinic-N, 24% pyrrolic-N and 7% graphitic-N whereas the activated BN-CSs had 19% pyridinic-N, 40% pyrrolic-N and 22% graphitic-N displaying the effect of activation on the type of N configurations in BN-CSs.

Green and scalable synthesis of 3D porous carbons microstructures as electrode materials for high rate capability supercapacitors.

Porous carbon nanostructures have long been studied because of their importance in many natural phenomena and their use in numerous applications. A more recent development is the ability to produce porous carbon materials with tuneable properties for electrochemical applications, which has enabled new research directions towards the production of suitable carbon materials for energy storage applications. Thus, this work explores the activation of carbon from polyaniline (PANI) using a less-corrosive potassium carbonate (KCO) salt, with different mass ratios of PANI and the activating agent (KCO as compared to commonly used KOH).

Correction: A high energy density asymmetric supercapacitor utilizing a nickel phosphate/graphene foam composite as the cathode and carbonized iron cations adsorbed onto polyaniline as the anode.

[This corrects the article DOI: 10.1039/C7RA12028A.].

A high energy density asymmetric supercapacitor utilizing a nickel phosphate/graphene foam composite as the cathode and carbonized iron cations adsorbed onto polyaniline as the anode.

This work presents the effect of different contents of graphene foam (GF) on the electrochemical capacitance of nickel phosphate Ni(PO) nano-rods as an electrode material for hybrid electrochemical energy storage device applications. Pristine Ni(PO) nano-rods and Ni(PO)/GF composites with different GF mass loadings of 30, 60, 90 and 120 mg were synthesised a hydrothermal method. The electrochemical behavior of pristine Ni(PO) and Ni(PO)/GF composites were analysed in a three-electrode cell configuration using 6 M KOH electrolyte.

Hydrothermal synthesis of manganese phosphate/graphene foam composite for electrochemical supercapacitor applications.

Manganese phosphate (Mn(PO) hexagonal micro-rods and (Mn(PO) with different graphene foam (GF) mass loading up to 150mg were prepared by facile hydrothermal method. The characterization of the as-prepared samples proved the successful synthesis of Mn(PO) hexagonal micro-rods and Mn(PO)/GF composites. It was observed that the specific capacitance of Mn(PO)/GF composites with different GF mass loading increases with mass loading up to 100mg, and then decreases with increasing mass loading up to 150mg.

Complete Genome of the Solvent-Tolerant Staphylococcus warneri Strain SG1.

Staphylococcus warneri is a Gram-positive bacterium commonly found in human skin flora. The genome of a laboratory S. warneri isolate, strain SG1, was sequenced to explore its mechanism of solvent tolerance and its potential as a chassis for biofuel production.

Expression of Saccharomyces cerevisiae Sdh3p and Sdh4p paralogs results in catalytically active succinate dehydrogenase isoenzymes.

Succinate dehydrogenase (SDH), also known as complex II, is required for respiratory growth; it couples the oxidation of succinate to the reduction of ubiquinone. The enzyme is composed of two domains. A membrane-extrinsic catalytic domain composed of the Sdh1p and Sdh2p subunits harbors the flavin and iron-sulfur cluster cofactors.

The Saccharomyces cerevisiae succinate dehydrogenase does not require heme for ubiquinone reduction.

The coupling of succinate oxidation to the reduction of ubiquinone by succinate dehydrogenase (SDH) constitutes a pivotal reaction in the aerobic generation of energy. In Saccharomyces cerevisiae, SDH is a tetramer composed of a catalytic dimer comprising a flavoprotein subunit, Sdh1p and an iron-sulfur protein, Sdh2p and a heme b-containing membrane-anchoring dimer comprising the Sdh3p and Sdh4p subunits. In order to investigate the role of heme in SDH catalysis, we constructed an S.

The role of Sdh4p Tyr-89 in ubiquinone reduction by the Saccharomyces cerevisiae succinate dehydrogenase.

Succinate dehydrogenase (complex II or succinate:ubiquinone oxidoreductase) is a tetrameric, membrane-bound enzyme that catalyzes the oxidation of succinate and the reduction of ubiquinone in the mitochondrial respiratory chain. Two electrons from succinate are transferred one at a time through a flavin cofactor and a chain of iron-sulfur clusters to reduce ubiquinone to an ubisemiquinone intermediate and to ubiquinol. Residues that form the proximal quinone-binding site (Q(P)) must recognize ubiquinone, stabilize the ubisemiquinone intermediate, and protonate the ubiquinone to ubiquinol, while minimizing the production of reactive oxygen species.

Identification of the heme axial ligands in the cytochrome b562 of the Saccharomyces cerevisiae succinate dehydrogenase.

Succinate dehydrogenase (SDH) plays a key role in energy generation by coupling the oxidation of succinate to the reduction of ubiquinone in the mitochondrial electron transport chain. The Saccharomyces cerevisiae SDH is composed of a catalytic dimer of the Sdh1p and Sdh2p subunits containing flavin adenine dinucleotide (FAD) and iron-sulfur clusters and a heme b-containing membrane-anchoring domain comprised of the Sdh3p and Sdh4p subunits. We systematically mutated all the histidine and cysteine residues in Sdh3p and Sdh4p to identify the residues involved in axial heme ligation.

The quaternary structure of the Saccharomyces cerevisiae succinate dehydrogenase. Homology modeling, cofactor docking, and molecular dynamics simulation studies.

Succinate dehydrogenases and fumarate reductases are complex mitochondrial or bacterial respiratory chain proteins with remarkably similar structures and functions. Succinate dehydrogenase oxidizes succinate and reduces ubiquinone using a flavin adenine dinucleotide cofactor and iron-sulfur clusters to transport electrons. A model of the quaternary structure of the tetrameric Saccharomyces cerevisiae succinate dehydrogenase was constructed based on the crystal structures of the Escherichia coli succinate dehydrogenase, the E.

The Saccharomyces cerevisiae mitochondrial succinate:ubiquinone oxidoreductase.

The Saccharomyces cerevisiae succinate dehydrogenase (SDH) provides an excellent model system for studying the assembly, structure, and function of a mitochondrial succinate:quinone oxidoreductase. The powerful combination of genetic and biochemical approaches is better developed in yeast than in other eukaryotes. The yeast protein is strikingly similar to other family members in the structural and catalytic properties of its subunits.

The Quinone-binding sites of the Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase.

The Saccharomyces cerevisiae succinate dehydrogenase (SDH) of the mitochondrial electron transport chain oxidizes succinate and reduces ubiquinone. Using a random mutagenesis approach, we identified functionally important amino acid residues in one of the anchor subunits, Sdh4p. We analyzed three point mutations (F69V, S71A, and H99L) and one nonsense mutation (Y89OCH) that truncates the Sdh4p subunit at the third predicted transmembrane segment.

The Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase. Identification of Sdh3p amino acid residues involved in ubiquinone binding.

Succinate dehydrogenase (SDH) participates in the mitochondrial electron transport chain by oxidizing succinate to fumarate and transferring the electrons to ubiquinone. In yeast, it is composed of a catalytic dimer, comprising the Sdh1p and Sdh2p subunits, and a membrane domain, comprising two smaller hydrophobic subunits, Sdh3p and Sdh4p, which anchor the enzyme to the mitochondrial inner membrane. To investigate the role of the Sdh3p anchor polypeptide in enzyme assembly and catalysis, we isolated and characterized seven mutations in the SDH3 gene.

The Saccharomyces cerevisiae succinate dehydrogenase anchor subunit, Sdh4p: mutations at the C-terminal lys-132 perturb the hydrophobic domain.

The yeast succinate dehydrogenase (SDH) is a tetramer of non-equivalent subunits, Sdh1p-Sdh4p, that couples the oxidation of succinate to the transfer of electrons to ubiquinone. One of the membrane anchor subunits, Sdh4p, has an unusual 30 amino acid extension at the C-terminus that is not present in SDH anchor subunits of other organisms. We identify Lys-132 in the Sdh4p C-terminal region as necessary for enzyme stability, ubiquinone reduction, and cytochrome b562 assembly in SDH.

The Saccharomyces cerevisiae succinate-ubiquinone reductase contains a stoichiometric amount of cytochrome b562.

The Saccharomyces cerevisiae succinate-ubiquinone reductase or succinate dehydrogenase (SDH) is a tetramer of non-equivalent subunits encoded by the SDH1, SDH2, SDH3, and SDH4 genes. In most organisms, SDH contains one or two endogenous b-type hemes. However, it is widely believed that the yeast SDH does not contain heme.

The carboxyl terminus of the Saccharomyces cerevisiae succinate dehydrogenase membrane subunit, SDH4p, is necessary for ubiquinone reduction and enzyme stability.

The succinate dehydrogenase (SDH) of Saccharomyces cerevisiae is composed of four nonidentical subunits encoded by the nuclear genes SDH1, SDH2, SDH3, and SDH4. The hydrophilic subunits, SDH1p and SDH2p, comprise the catalytic domain involved in succinate oxidation. They are anchored to the inner mitochondrial membrane by two small, hydrophobic subunits, SDH3p and SDH4p, which are required for electron transfer and ubiquinone reduction.