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  • Electronic Resource  (3)
  • Nuclease  (2)
  • Hexanuclear zirconium cluster  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of cluster science 9 (1998), S. 63-91 
    ISSN: 1572-8862
    Keywords: Hexanuclear zirconium cluster ; pentanuclear zirconium cluster ; cluster hydrogen atom ; bromide ; chloride ; arsine ; amine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract Reduction of ZrBr4 with HSnBu3 yielded a blue solid. When this blue solid was treated with PMe3, a hexanuelear cluster [Zr6Br14H4( PMe3)4] (2) was isolated. Reaction of the blue solid with [PPh4]Br in CH2Cl2 resulted in the formation of a paramagnetic and unstable cluster anion, [Zr6Br18H5]2− (3′), which disproportionated to form a new cluster anion, [Zr6Br18H5]3− (4′) and some Zr(IV) species. Compounds containing 4′ can also be obtained from reaction of the blue solid with Br− in MeCN. Reduction of ZrCl4 with HsnBu3 gave a red–brown solid, and [Zr6Cl14H4(AsMe3)4] (9) and [Zr5Cl12H4(AsMe3)5](8) were obtained by reaction of the red–brown solid with AsMe3. No cluster compounds containing amine ligands were obtained in the reaction of the red–brown solid with amines; only compounds containing the [Zr6Cl18 H5]3− anion and ammonium cations were isolated. Altogether ten products were characterized by single crystal X-ray diffraction and where possible, by 1H NMR studies.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4919
    Keywords: Nuclease ; Staphylococcal Nuclease ; Micrococcal Nuclease ; Enzyme Function and Structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary This is the second of a series of four articles in which the chemical, enzymological and crystallographic work on Ribonucleate (deoxyribonucleate)-3′-nucleotidohydrolase EC 3.1.4.4 (staphylococcal nuclease, micrococcal nuclease) will be reviewed and correlated. This article discusses studies in solution delineating the extent of the binding site of the enzyme and identifying some of the particular amino acid residues that form this site. In addition, the effects of the very potent inhibitory combination of thymidine-3′,5′-diphosphate and Ca2+ on the conformation of the enzyme and its physical, chemical and enzymological properties will be reviewed.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 23 (1979), S. 131-141 
    ISSN: 1573-4919
    Keywords: Nuclease ; Staphylococcal Nuclease ; Micrococcal Nuclease ; Protein Folding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary This is the last in a series of four articles in which the chemical, enzymological and crystallographic work on Ribonucleate (deoxyribonucleate)-3′-nucleotidohydrolase, EC 3.1.4.4 (staphylococcal nuclease, micrococcal nuclease) will be reviewed and correlated. This article discusses the use of the nuclease as a model system for the study of the mechanisms and energetics of the folding-unfolding reaction in proteins and for the study of the interrelationships between amino acid sequence and three-dimensional structure.
    Type of Medium: Electronic Resource
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