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  • ARA06C Expedtion; Chukchi Sea; Headspace Gas; pore water; TOC  (1)
  • Alcohol dehydrogenase  (1)
  • Barium; Boron; Bromine; CAGE; Calcium; Center for Marine Environmental Sciences; Centre for Arctic Gas Hydrate, Environment and Climate; Chlorine; DEPTH, sediment/rock; GC; GeoB21601-1; Gravity corer; Iron; Lithium; Magnesium; Manganese; Maria S. Merian; MARUM; MSM57/1; MSM57/1_613-1; Optional event label; Potassium; Silicon; Sodium; Strontium; Sulfate  (1)
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  • 1
    Publikationsdatum: 2024-04-27
    Beschreibung: Here we represent pore water, headspace gas, and TOC data from the four cores recovered from the Chukchi Sea by Jumbo Piston Corer (JPC) during the ARA06C Expedition in 2015 to investigate the origin and diagenesis of pore water and gas. The study cores were retrieved from the Chukchi Sea Shelf (ARA06C-JPC01), the Northwind Basin (ARA06C-JPC02), the East Siberia Continental Slope (ARA06C-JPC03), and the Chukchi Basin (ARA06C-JPC04). We collected pore water from Site ARA06C-JPC01, ARA06C-JPC02, ARA06C-JPC03, and ARA06C-JPC04 and performed compositional and isotopic analyses (e.g. major cation and anions, oxygen, and deuterium isotope, carbon-13 isotope of dissolved carbon, 87Sr/86Sr). The analyzed results of pore water were displayed in the PW Table. The compositional and isotopic data of headspace gas (e.g. methane concentration, and carbon-13 isotope of methane and carbon dioxide) from Site ARA06C-JPC01, ARA06C-JPC02, ARA06C-JPC03, and ARA06C-JPC04 as well as TOC content of bulk sediment from Site ARA06C-JPC01, were represented in the HS Table and TOC Table, respectively.
    Schlagwort(e): ARA06C Expedtion; Chukchi Sea; Headspace Gas; pore water; TOC
    Materialart: Dataset
    Format: application/zip, 3 datasets
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Publikationsdatum: 2024-06-26
    Schlagwort(e): Barium; Boron; Bromine; CAGE; Calcium; Center for Marine Environmental Sciences; Centre for Arctic Gas Hydrate, Environment and Climate; Chlorine; DEPTH, sediment/rock; GC; GeoB21601-1; Gravity corer; Iron; Lithium; Magnesium; Manganese; Maria S. Merian; MARUM; MSM57/1; MSM57/1_613-1; Optional event label; Potassium; Silicon; Sodium; Strontium; Sulfate
    Materialart: Dataset
    Format: text/tab-separated-values, 378 data points
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Springer
    Journal of molecular evolution 34 (1992), S. 522-535 
    ISSN: 1432-1432
    Schlagwort(e): Alcohol dehydrogenase ; Molecular evolution ; Sequence alignment ; Phylogenetic tree ; Structure and function of proteins
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary Sequences of 47 members of the Zn-containing alcohol dehydrogenase (ADH) family were aligned progressively, and an evolutionary tree with detailed branch order and branch lengths was produced. The alignment shows that only 9 amino acid residues (of 374 in the horse liver ADH sequence) are conserved in this family; these include eight Gly and one Val with structural roles. Three residues that bind the catalytic Zn and modulate its electrostatic environment are conserved in 45 members. Asp 223, which determines specificity for NAD, is found in all but the two NADP-dependent enzymes, which have Gly or Ala. Ser or Thr 48, which makes a hydrogen bond to the substrate, is present in 46 members. The four Cys ligands for the structural zinc are conserved except in ζ-crystallin, the sorbitol dehydrogenases, and two bacterial enzymes. Analysis of the evolutionary tree gives estimates of the times of divergence for different animal ADHs. The human class II (π) and class III (κ) ADHs probably diverged about 630 million years ago, and the newly identified human ADH6 appeared about 520 million years ago, implying that these classes of enzymes may exist or have existed in all vertebrates. The human class I ADH isoenzymes (α, β, and γ) diverged about 80 million years ago, suggesting that these isoenzymes may exist or have existed in all primates. Analysis of branch lengths shows that these plant ADHs are more conserved than the animal ones and that class III ADHs are more conserved than class I ADHs. The rate of acceptance of point mutations (PAM units) shows that selection pressure has existed for ADHs, implying that these enzymes play definite metabolic roles.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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