Herein, CoCrCuFeMnNi (x = 0, 0.5, 1.0, 1.5, and 2.0, in molar ratio) high-entropy alloys (HEAs) are fabricated by vacuum hot-pressing sintering (VHPS). The effect of Cr content on the microstructure and oxidation behavior are studied. When x ≤ 1.5 mol, the phases of the four alloys were all composed of FCC2 major phase and FCC1 secondary phase, while Cr alloy consisted of a small amount of FCC1 phase and ρ phase in addition to FCC2 main phase. The elemental segregation increased with the increase of Cr content. Cr alloy exhibited the lowest oxidation rate constants in the oxidation stage and the slow oxidation stage, which were 2.29 × 10 and 3.46 × 10 g cm s, respectively, showing the best oxidation resistance. The oxidation products of CoCrCuFeMnNi HEA system were mainly MnO, MnO, CrO and (M,Cr)O-type spinel oxides. The oxidation mechanism is mainly selective oxidation, that is, the outward diffusion of metal cations and the inward diffusion of oxygen ions. The oxidation resistance of the Cr-rich FCC1 and ρ phases is better than that of the copper-rich FCC2 phase.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1016/j.micron.2022.103291 | DOI Listing |
Proc Natl Acad Sci U S A
January 2025
Department of Bioengineering, California Institute of Technology, Pasadena, CA 91125.
The diversity and heterogeneity of biomarkers has made the development of general methods for single-step quantification of analytes difficult. For individual biomarkers, electrochemical methods that detect a conformational change in an affinity binder upon analyte binding have shown promise. However, because the conformational change must operate within a nanometer-scale working distance, an entirely new sensor, with a unique conformational change, must be developed for each analyte.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
January 2025
California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720.
Polysaccharide monooxygenase (PMO) catalysis involves the chemically difficult hydroxylation of unactivated C-H bonds in carbohydrates. The reaction requires reducing equivalents and will utilize either oxygen or hydrogen peroxide as a cosubstrate. Two key mechanistic questions are addressed here: 1) How does the enzyme regulate the timely and tightly controlled electron delivery to the mononuclear copper active site, especially when bound substrate occludes the active site? and 2) How does this electron delivery differ when utilizing oxygen or hydrogen peroxide as a cosubstrate? Using a computational approach, potential paths of electron transfer (ET) to the active site copper ion were identified in a representative AA9 family PMO from (PMO9E).
View Article and Find Full Text PDFProc Natl Acad Sci U S A
January 2025
School of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong 10120, Thailand.
A single-component flavin-dependent halogenase, AetF, has emerged as an attractive biocatalyst for catalyzing halogenation. However, its flavin chemistry remains unexplored and cannot be predicted due to its uniqueness in sequence and structure compared to other flavin-dependent monooxygenases. Here, we investigated the flavin reactions of AetF using transient kinetics.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
January 2025
Ministry of Education Key Laboratory of Environment Remediation and Ecological Health, Zhejiang Provincial Key Laboratory of Agricultural Resources and Environment, College of Environmental and Resource Sciences, Zhejiang University, Hangzhou 310058, China.
While iron (Fe) is essential for life and plays important roles for almost all growth related processes, it can trigger cell death in both animals and plants. However, the underlying mechanisms for Fe-induced cell death in plants remain largely unknown. S-nitrosoglutathione reductase (GSNOR) has previously been reported to regulate nitric oxide homeostasis to prevent Fe-induced cell death within root meristems.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
January 2025
Department of Biology, Faculty of Science and Technology, Mount Royal University, Calgary, AB T3E 6K6, Canada.
With over 14 million people living above 3,500 m, the study of acclimatization and adaptation to high altitude in human populations is of increasing importance, where exposure to high altitude (HA) imposes a blood oxygenation and acid-base challenge. A sustained and augmented hypoxic ventilatory response protects oxygenation through ventilatory acclimatization, but elicits hypocapnia and respiratory alkalosis. A subsequent renally mediated compensatory metabolic acidosis corrects pH toward baseline values, with a high degree of interindividual variability.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!