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1.
ACS Nano ; 18(36): 25046-25052, 2024 Sep 10.
Article in English | MEDLINE | ID: mdl-39178239

ABSTRACT

van der Waals (vdW) layered materials have been shown to have excellent optoelectronic properties relevant to photovoltaics. Despite their promise, the demonstrated efficiencies of vdW material solar cells remain low and are seldom supported by statistics or spectral quantum efficiency analysis. In this study, we utilize a p-type WSe2 absorber, forming a solar cell with a transparent front InOx electron contact, and a rear Pd reflector/hole contact. We fabricate multiple devices providing statistics for 10 devices with an average 1 sun conversion efficiency above 5%, among which a champion efficiency of 6.37% is achieved. This is the highest AM 1.5G 1 sun efficiency reported for a vdW material solar cell, with a current density supported by external quantum efficiency analysis. This cell is also shown to have near unity quantum efficiency around λ = 600 nm. This work provides support to vdW materials being considered as serious candidates for future thin-film solar cells.

2.
Nano Converg ; 11(1): 25, 2024 Jun 27.
Article in English | MEDLINE | ID: mdl-38937391

ABSTRACT

Two-dimensional (2D) materials have emerged as promising building blocks for next generation memristive devices, owing to their unique electronic, mechanical, and thermal properties, resulting in effective switching mechanisms for charge transport. Memristors are key components in a wide range of applications including neuromorphic computing, which is becoming increasingly important in artificial intelligence applications. Crossbar arrays are an important component in the development of hardware-based neural networks composed of 2D materials. In this paper, we summarize the current state of research on 2D material-based memristive devices utilizing different switching mechanisms, along with the application of these devices in neuromorphic crossbar arrays. Additionally, we discuss the challenges and future directions for the field.

3.
FEBS J ; 291(9): 1992-2008, 2024 May.
Article in English | MEDLINE | ID: mdl-38362806

ABSTRACT

The nucleoside inosine is a main intermediate of purine nucleotide catabolism in Saccharomyces cerevisiae and is produced via the dephosphorylation of inosine monophosphate (IMP) by IMP-specific 5'-nucleotidase 1 (ISN1), which is present in many eukaryotic organisms. Upon transition of yeast from oxidative to fermentative growth, ISN1 is important for intermediate inosine accumulation as purine storage, but details of ISN1 regulation are unknown. We characterized structural and kinetic behavior of ISN1 from S. cerevisiae (ScISN1) and showed that tetrameric ScISN1 is negatively regulated by inosine and adenosine triphosphate (ATP). Regulation involves an inosine-binding allosteric site along with IMP-induced local and global conformational changes in the monomer and a tetrameric re-arrangement, respectively. A proposed interaction network propagates local conformational changes in the active site to the intersubunit interface, modulating the allosteric features of ScISN1. Via ATP and inosine, ScISN1 activity is likely fine-tuned to regulate IMP and inosine homeostasis. These regulatory and catalytic features of ScISN1 contrast with those of the structurally homologous ISN1 from Plasmodium falciparum, indicating that ISN1 enzymes may serve different biological purposes in different organisms.


Subject(s)
Adenosine Triphosphate , Allosteric Site , Inosine , Saccharomyces cerevisiae Proteins , Saccharomyces cerevisiae , Saccharomyces cerevisiae/genetics , Saccharomyces cerevisiae/enzymology , Saccharomyces cerevisiae/metabolism , Adenosine Triphosphate/metabolism , Inosine/metabolism , Kinetics , Saccharomyces cerevisiae Proteins/metabolism , Saccharomyces cerevisiae Proteins/genetics , Saccharomyces cerevisiae Proteins/chemistry , Catalytic Domain , Allosteric Regulation , Crystallography, X-Ray , Inosine Monophosphate/metabolism , Models, Molecular , Protein Conformation , Protein Binding
4.
J Biol Chem ; 298(5): 101869, 2022 05.
Article in English | MEDLINE | ID: mdl-35346685

ABSTRACT

Pseudouridine, one major RNA modification, is catabolized into uracil and ribose-5'-phosphate by two sequential enzymatic reactions. In the first step, pseudouridine kinase (PUKI) phosphorylates pseudouridine to pseudouridine 5'-monophosphate. High-fidelity catalysis of pseudouridine by PUKI prevents possible disturbance of in vivo pyrimidine homeostasis. However, the molecular basis of how PUKI selectively phosphorylates pseudouridine over uridine with >100-fold greater efficiency despite minor differences in their Km values has not been elucidated. To investigate this selectivity, in this study we determined the structures of PUKI from Escherichia coli strain B (EcPUKI) in various ligation states. The structure of EcPUKI was determined to be similar to PUKI from Arabidopsis thaliana, including an α/ß core domain and ß-stranded small domain, with dimerization occurring via the ß-stranded small domain. In a binary complex, we show that Ser30 in the substrate-binding loop of the small domain mediates interactions with the hallmark N1 atom of pseudouridine nucleobase, causing conformational changes in its quaternary structure. Kinetic and fluorescence spectroscopic analyses also showed that the Ser30-mediated interaction is a prerequisite for conformational changes and subsequent catalysis by EcPUKI. Furthermore, S30A mutation or EcPUKI complexed with other nucleosides homologous to pseudouridine but lacking the pseudouridine-specific N1 atom did not induce such conformational changes, demonstrating the catalytic significance of the proposed Ser30-mediated interaction. These analyses provide structural and functional evidence for a pseudouridine-dependent conformational change of EcPUKI and its functional linkage to catalysis.


Subject(s)
Arabidopsis , Escherichia coli/enzymology , Pseudouridine , Biocatalysis , Catalysis , Kinetics , Uridine
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