Plasmonic enhanced dye-sensitized solar cells (DSSCs) with metallic nanostructures suffer from corrosion problems, especially with the presence of the iodine/triiodide redox couple in the electrolyte. Herein, we introduce an alternative approach by compensating the corrosion with a modified liquid electrolyte. In contrast to the existing method of surface preservation for plasmonic nanostructures, the redox-controlled electrolyte (RCE) contains iodoaurate intermediates, i.e. gold(i) diiodide (AuI) and gold(iii) tetraiodide (AuI) with optimal concentrations, such that these intermediates are readily reduced to gold nanoparticles during the operation of DSSCs. As corrosion and redeposition of gold occur simultaneously, it effectively provides corrosion compensation to the plasmonic gold nanostructures embedded in the photoanode. Cycling tests of the specific amount of gold contents in the RCE of DSSCs support the fact that the dissolution and deposition of gold are reversible and repeatable. This gold deposition on the TiO photoanode results in forming a Schottky barrier (SB) at the metal-semiconductor interface and effectively inhibits the recombination of electron-hole pairs. Therefore, the RCE increases the short-circuit current, amplifies the open-circuit voltage, and reduces the impedance of the TiO/dye interface. The power conversion efficiency of DSSCs was improved by 57% after incorporating the RCE.
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http://dx.doi.org/10.1039/c7nr03506c | DOI Listing |
J Cell Sci
September 2022
School of Basic Medical Sciences, Anhui Medical University, Hefei, Anhui 230032, China.
Swift and complete spindle disassembly in late mitosis is essential for cell survival, yet how it happens is largely unknown in mammalian cells. Here we used real-time live cell microscopy and biochemical assays to show that the primordial dwarfism (PD)-related cysteine-rich protein CRIPT dictates the spindle disassembly in a redox-dependent manner in human cells. This previously reported cytoplasmic protein was found to have a confined nuclear localization with a nucleolar concentration during interphase but was distributed to spindles and underwent redox modifications to form disulfide bonds in CXXC pairs during mitosis.
View Article and Find Full Text PDFElife
September 2022
Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, Stockholm, Sweden.
Redox reactions are central to biochemistry and are both controlled by and induce protein structural changes. Here, we describe structural rearrangements and crosstalk within the ribonucleotide reductase R2b-NrdI complex, a di-metal carboxylate-flavoprotein system, as part of the mechanism generating the essential catalytic free radical of the enzyme. Femtosecond crystallography at an X-ray free electron laser was utilized to obtain structures at room temperature in defined redox states without suffering photoreduction.
View Article and Find Full Text PDFEnviron Toxicol Chem
November 2022
Department of Chemistry and Biochemistry, Wilfrid Laurier University, Waterloo, Ontario, Canada.
The controls governing the availability of reduced selenium (Se) species, namely selenite (Se[IV]) and dissolved organo-Se (DOSe), to primary producers at the sediment-water interface in depositional environments (i.e., lentic systems) were assessed through consideration of theoretical principles and field data.
View Article and Find Full Text PDFOrg Biomol Chem
April 2022
Department of Chemistry, Indian Institute of Engineering Science and Technology, Shibpur, Botanic Garden, Howrah 711103, India.
Herein, we report ligand-centered redox controlled Zn(II)-catalyzed multicomponent approaches for synthesizing pyrimidines and triazines. Taking advantage of the ligand-centered redox events and using a well-defined Zn(II)-catalyst (1a) bearing ()-2-((4-chlorophenyl)diazenyl)-1,10-phenanthroline (L1a) as the redox-active ligand, a wide variety of substituted pyrimidines and triazines were prepared dehydrogenative alcohol functionalization reactions. Pyrimidines were prepared two pathways: (i) dehydrogenative coupling of primary and secondary alcohols with amidines and (ii) dehydrogenative coupling of primary alcohols with alkynes and amidines.
View Article and Find Full Text PDFNat Commun
April 2021
Department of Biochemistry and Molecular Biology, 985870 Nebraska Medical Center, Omaha, NE, USA.
Human manganese superoxide dismutase is a critical oxidoreductase found in the mitochondrial matrix. Concerted proton and electron transfers are used by the enzyme to rid the mitochondria of O. The mechanisms of concerted transfer enzymes are typically unknown due to the difficulties in detecting the protonation states of specific residues and solvent molecules at particular redox states.
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