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- Ivanov, I. I., et al.
(författare)
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Investigation of catalytic hydrogen sensors with platinum group catalysts
- 2021
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Ingår i: Sensors and actuators. B, Chemical. - : Elsevier. - 0925-4005 .- 1873-3077. ; 346
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Tidskriftsartikel (refereegranskat)abstract
- Environmental deterioration and limited resources of hydrocarbons push the development of alternative power sources. One of the most promising energy carriers is hydrogen. However, handling hydrogen is more hazardous than the use of hydrocarbons because it has a significantly wider flammable range. Thus the development of new sensors for preventing hydrogen leakage is the actual task of modern materials science and chemical engineering. In this work, the response of catalytic sensors to hydrogen with different catalysts of platinum group (Pt, Pd, Ir, Rh, Pt + Pd, Pt + Pd + Rh, Pt + Pd + Ir) in the pre-explosion concentration range is studied. Temperature dependencies of sensitivity are discussed. A hysteresis in sensor response is observed during the cycling of the supply voltage. This phenomenon can be explained by partial transformation of platinum group metal oxides into metallic phase at a temperature of more than 500 °C and reverse metal oxidation at temperatures less than 400 °C. It has been shown that the sensors with catalysts containing Ir and Rh demonstrate more preferable characteristics for practical applications. © 2021 Elsevier B.V.
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- Drobysheva, Arina V., et al.
(författare)
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Structure and function of virion RNA polymerase of a crAss-like phage
- 2021
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Ingår i: Nature. - : Nature Publishing Group. - 0028-0836 .- 1476-4687. ; 589:7841, s. 306-309
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Tidskriftsartikel (refereegranskat)abstract
- The RNA polymerase from the crAss-like bacteriophage phi14:2, which is translocated into the host cell with phage DNA and transcribes early phage genes, is structurally most similar to eukaryotic RNA interference polymerases, suggesting that the latter have a phage origin. CrAss-like phages are a recently described expansive group of viruses that includes the most abundant virus in the human gut(1-3). The genomes of all crAss-like phages encode a large virion-packaged protein(2,4) that contains a DFDxD sequence motif, which forms the catalytic site in cellular multisubunit RNA polymerases (RNAPs)(5). Here, using Cellulophaga baltica crAss-like phage phi14:2 as a model system, we show that this protein is a DNA-dependent RNAP that is translocated into the host cell along with the phage DNA and transcribes early phage genes. We determined the crystal structure of this 2,180-residue enzyme in a self-inhibited state, which probably occurs before virion packaging. This conformation is attained with the help of a cleft-blocking domain that interacts with the active site and occupies the cavity in which the RNA-DNA hybrid binds. Structurally, phi14:2 RNAP is most similar to eukaryotic RNAPs that are involved in RNA interference(6,7), although most of the phi14:2 RNAP structure (nearly 1,600 residues) maps to a new region of the protein fold space. Considering this structural similarity, we propose that eukaryal RNA interference polymerases have their origins in phage, which parallels the emergence of the mitochondrial transcription apparatus(8).
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