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  • 1
    Online Resource
    Online Resource
    Raw Materials for Future Energy Supply (2019)
    Cham : Springer
    Details Availability
    Keywords: Earth sciences ; Renewable energy sources ; Alternate energy sources ; Green energy industries ; Earth Sciences ; Earth sciences ; Renewable energy sources ; Alternate energy sources ; Green energy industries ; Renewable energy resources ; Economic geology ; Geobiology ; Renewable energy resources ; Economic geology ; Geobiology ; Force and energy. ; Materials science. ; Welt ; Rohstoffversorgung ; Natürliche Ressourcen ; Erneuerbare Energien ; Energiewirtschaft ; Energieversorgung ; Rohstoff ; Rohstoffbedarf ; Rohstoffverbrauch ; Energiewende ; Energieversorgung ; Rohstoffbedarf ; Wertstoff ; Strategischer Rohstoff ; Seltenerdmetall ; Erneuerbare Energien ; Kritischer Rohstoff ; Mineralischer Rohstoff
    Description / Table of Contents: This is the first book that analyses the future raw materials supply from the demand side of a society that chiefly relies on renewable energies, which is of great significance for us all. It addresses primary and secondary resources and substitution, not only from technical but also socioeconomic and ethical points of view. The “Energiewende” (Energy Transition) will change our consumption of natural resources significantly. When in future our energy requirements will be covered mostly by wind, solar power and biomass, we will need less coal, oil and natural gas. However, the consumption of minerals, especially metallic resources, will increase to build wind generators, solar panels or energy storage facilities. Besides e.g. copper, nickel or cobalt, rare earth elements and other high-tech elements will be increasingly used. With regard to primary metals, Germany is 100 % import dependent; only secondary material is produced within Germany. Though sufficient geological primary resources exist worldwide, their availability on the market is crucial. The future supply of the market is dependent on the development of prices, the transparency of the market and the question of social and ethical standards in the raw materials industry, as well as the social license to operate, which especially applies to mining. The book offers a valuable resource for everyone interested in the future raw material supply of our way of life, which will involve more and more renewable energies
    Type of Medium: Online Resource
    Pages: Online-Ressource (XXX, 225 p. 53 illus. in color, online resource)
    ISBN: 9783319912295
    Series Statement: SpringerLink
    URL: http://dx.doi.org/10.1007/978-3-319-91229-5
    URL: https://doi.org/10.1007/978-3-319-91229-5
    DOI: 10.1007/978-3-319-91229-5
    RVK:
    RB 10699
    Language: English
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  • 2
    Electronic Resource
    Electronic Resource
    Zur Kenntnis des Faktors F430 aus methanogenen Bakterien: Über die Natur der Isolierungsartefakte von F430, ein Beitrag zur Chemie von F430 und zur konformationellen Stereochemie der Ligandperipherie von hydroporphinoiden Nickel(II)-Komplexen (1985)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 68 (1985), S. 1338-1358 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Factor F430 from Methanogenic Bacteria: On the Nature of the Isolation Artefacts of F430, a Contribution to the Chemistry of F430 and the Conformational Stereochemistry of the Ligand Periphery of Hydroporphinoid Nickel(II) ComplexesFactor F430 (1), a coenzyme from methanogenic bacteria, when heated in aqueous solution isomerizes to 12,13-di-epi-F430 (5) via 13-epi-F430 (3). The equilibrium mixture of the three F430 isomers in aqueous phosphate buffer solution (pH 7, 100°) contains 88 % of 5, 8 % of 3, and 4 % of 1 (Scheme 1). The structural assignment for the F430 isomers rests on FAB-MS-, UV/VIS-, 1H- and 13C-NMR spectra of their pentamethyl esters. Chemical proof for the double epimerization at the two chiral centers of F430's ring C was provided by ozonolytic degradation of the di-epimer to give a ring-C-derived succinimide derivative that was shown to be the enantiomer of the one previously obtained by ozonolysis of F430M (see Scheme 2). The two F430 ring-C epimers 3 and 5 are the isolation artefacts described in the earlier F430 literature. F430 is susceptible to autoxidation in air and the product, that absorbs at 560 nm, was shown to be the 12,13-didehydro derivative 8 of F430 by spectroscopic characterization of its pentamethyl ester 9. The dehydrogenation product 8 can be diastereoselectively reduced with Zn in AcOH to give natural F430 as the main product rather than the thermodynamically more stable F430-di-epimer (Scheme 3). In the double epimerization of F430, the two ring-C side chains change from a trans-quasi-diaxial arrangement to the (locally) enantiomorphic position in which the same side chains are again in a trans-quasi-diaxial arrangement. This equilibrium paradox as well as the kinetic diastereoselectivity of the reduction of 12,13-didehydro-F430 (8) are rationalized to be consequences of the general phenomenon documented earlier (see the preceding paper) according to which hydroporphinoid Ni(II) complexes all show a characteristic conformational ruffling of their ligand system due to the tendency of the (small) Ni(II) ion to contract the size of the ligand's central coordination hole (see Fig. 5 and 6).
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19850680527
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  • 3
    Electronic Resource
    Electronic Resource
    Zur Kenntnis des Faktors F430 aus methanogenen Bakterien: Struktur des proteinfreien Faktors (1984)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 67 (1984), S. 334-351 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Factor F430 from Methanogenic Bacteria: Structure of the Protein-free FactorFactor F430, the porphinoid nickel-containing coenzyme of the methylcoenzyme-M reductase of metanogenic bacteria is shown to be the 33,83,122,133,182-pentaacid derivative of the pentamethylester F430M, the structure of which had been determined previously (see structural formulae 1 and 2). The structure assignment rests on chromatographic, UV/VIS-, CD-, IR-, and 13C-NMR-spectroscopic as well as FAB-mass spectral comparision of F430 with F430M and the pentaacid prepared by acid-catalyzed hydrolysis of F430M.In the cells of Methanobacterium thermoautotrophicum, factor F430 is present in a ‘bound’ and also, depending on the growth conditions, in ‘free’ form, the latter being defined as the part of total F430 that can be extracted from the cells under extremely mild conditions (80% EtOH at 0-4°). From the (protein)-‘bound’ form, F430 is extracted by subsequently treating the cells at 0-4° with 80% EtOH containing (e.g.), 2m LiCi.From both sources, the extracted factor is the same pentaacid, and there is no indication for the existence of a protein-free F430 species that would contain additional (covalently bound) structural elements.
    Additional Material: 17 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19840670141
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  • 4
    Electronic Resource
    Electronic Resource
    Zur Kenntnis des Faktors F430 aus methanogenen Bakterien: Struktur des porphinoiden Ligandsystems (1982)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 65 (1982), S. 828-865 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Factor F430 from Methanogenic Bacteria: Structure of the Porphninoid Ligand SystemA structure is proposed for F430M, a non-cristalline methanolysis product of isolates of the nickel-containing, porphinoid factor F430 from Methanobacterium thermoautotrophicum.Crucial to the structure determination are five incorporation experiments with M. thermoautotrophicum (strain Marburg) in which the specifically mono-13C-labeled biosynthetic precursors (2-13C), (3-13C), (4-13C)-, (5-13C) ALA (ALA = δ-amino-levulinic acid) and L-(methyl-13C)methionine were incorporated into F430 with high efficiency. The 13C-NMR,-spectra of the specifically labeled F430M samples derived therefrom, together with the UV./VIS. spectral data of F430M, contain all the information necessary for the deduction of the constitution of the F430M chromophore, assuming the established pattern of porphinoid biosynthesis to be operative in F430 biosynthesis. 1H-NMR. spectroscopy and, in particular, 1H-NMR.-NOE-difference spectroscopy corroborates and completes the constitutional assignments and, furthermore, makes possible an almost complete derivation of the molecule's relative configuration. Schemes 3 and 4 summarize the results of 1H-NMR. spectroscopy, presenting them within the context of the proposed structure for F430M. The assignment of absolute configuration implied in the formula is given preference because of F430M's very close structural and (assumed) biosynthetic relationship to sirohydrochlorin and vitamin B12 (with respect to ring C, the assignment is based on degradative evidence).According to the proposed structure, the nickel complex F430M possesses an uroporphinoid (Type III) ligand skeleton with an additional carbocyclic ring and a chromophore system not previously encountered among natural porphinoids. It can be considered to be a (tetrahydro) derivative of the corphin system, combining structural elements of both porphyrins and corrins.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19820650320
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  • 5
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray diffraction studies of formylmethanofuran: Tetrahydromethanopterin formyltransferase from Methanopyrus kandleri (1996)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 26 (1996), S. 118-120 
    Details
    ISSN: 0887-3585
    Keywords: Protein crystallization ; X-ray crystallography ; methanogenic Archaea ; hyperthermophilic enzymes ; halophilic enzymes ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Formylmethanofuran:tetrahydromethanopterin formyltransferase from the hyperthermophilic methanogenic Archaeon Methanopyrus kandleri (growth temperature optimum 98°C) was crystallized by vapor diffusion methods. Crystal form M obtained with 2-methyl-2,4-pentanediol as precipitant displayed the space group P21 with unit cell parameters of a = 87.0 Å, b = 75.4 Å, c = 104.7 Å, and β = 113.9° and diffracted better than 2 Å resolution. Crystal form P grown from polyethylene glycol 8000 belonged to the space group I4122 and had unit cell parameters of 157.5 Å and 242.1 Å. Diffraction data to 1.73 Å were recorded. Crystal form S which was crystallized from (NH4)2SO4in the space group I4122 with unit cell parameters of 151.3 Å and 249.5 Å diffracted at least to 2.2 Å resolution. All crystal forms probably have four molecules per asymmetric unit and are suitable for X-ray structure analysis. © 1996 Wiley-Liss, Inc.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Zum Katalysemechanismus einer metallfreien Hydrogenase aus methanogenen Archaea: enzymatische Umsetzung von H2 ohne Metall und ihre Analogie zur Chemie der Alkane in supersaurer LösungDiese Arbeit wurde vom Bundesministerium für Forschung und Technologie (Förderprogramm „Biologische Wasserstoffgewinnung“) und vom Fonds der Chemischen Industrie gefördert. (1995)
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 107 (1995), S. 2418-2421 
    Details
    ISSN: 0044-8249
    Keywords: Archaebakterien ; Carbokationen ; Enzyme ; Hydrogenasen ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ange.19951072011
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  • 7
    Electronic Resource
    Electronic Resource
    On the Mechanism of Catalysis by a Metal-Free Hydrogenase from Methanogenic Archaea: Enzymatic Transformation of H2 without a Metal and Its Analogy to the Chemistry of Alkanes in Superacidic SolutionThis work was supported by the Bundesministerium für Forschung und Technologie (Förderprogramm “Biologische Wasserstoffgewinnung”) and by the Fonds der Chemischen Industrie. (1995)
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 34 (1995), S. 2247-2250 
    Details
    ISSN: 0570-0833
    Keywords: Archaea bacteria ; carbocations ; enzymes ; hydrogenases ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/anie.199522471
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