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  • 1
    ISSN: 0044-2313
    Keywords: Phosphorus nitrides ; nitrido sodalites ; transition metals ; synthesis ; structure ; i.r. data ; Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Nitrido-Sodalites. II. Synthesis, Crystal Structure, and Properties of M(6+(y/2)-x)H2x[P12N24]Zy with M = Fe, Co, Ni, Mn; Z = Cl, Br, I; 0 ≤ x ≤ 4; y ≤ 2The nitrido sodalites M(6+(y/2)-x)H2x[P12N24]Zy with M = Fe, Co, Ni, Mn; Z = Cl, Br, I; 0 ≤ x ≤ 4; y ≤ 2 are obtained by the reaction of HPN2 or [PN(NH2)2]3 with the metal halogenide MZ2 (T = 700°C). The compounds are isotypic to Zn(7-x)H2x[P12N24]Cl2. An increase of the ionic radii of the cations or anions results in an expansion of the lattice which is caused by an increase of the P—N—P angle. The influence of the cation is more dominant than that of the anion. By reacting [PN(NH2)2]3 with metal halogenide (MZ2) hydrogen free, X-ray amorphous products are obtained. The formation of the chloride-containing P—N-sodalite in this reaction begins at temperatures below 450°C.
    Notes: Die Nitrido-Sodalithe M(6+(y/2)-x)H2x[P12N24]Zy mit M = Fe, Co, Ni, Mn; Z = Cl, Br, I; 0 ≤ x ≤ 4; y ≤ 2 wurden durch Umsetzung von HPN2 bzw. von [PN(NH2)2]3 mit dem jeweiligen Metallhalogenid MZ2 hergestellt (T = 700°C). Sie sind mit Zn(7-x)H2x[P12N24]Cl2 isotyp. Mit steigendem Ionenradius von Kationen oder Anionen findet man eine Aufweitung des Volumens. Dies ist mit einer Vergrößerung des P—N—P-Winkels verbunden. Der Einfluß der Kationen ist dabei stärker als jener der Anionen. Durch Reaktion von [PN(NH2)2]3 mit dem jeweiligen Metallhalogenid MZ2 werden wasserstofffreie P—N-Sodalithe als röntgenamorphe Pulver erhalten. Bei diesen Reaktionen setzt die Bildung der chlorhaltigen P—N-Sodalithe schon unterhalb von 450°C ein.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-11-27
    Description: Adenosine triphosphate (ATP) synthase contains a rotary motor involved in biological energy conversion. Its membrane-embedded F0 sector has a rotation generator fueled by the proton-motive force, which provides the energy required for the synthesis of ATP by the F1 domain. An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits. Each c subunit forms an alpha-helical hairpin. The interhelical loops of six to seven of the c subunits are in close contact with the gamma and delta subunits of the central stalk. The extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stock, D -- Leslie, A G -- Walker, J E -- New York, N.Y. -- Science. 1999 Nov 26;286(5445):1700-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10576729" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Catalysis ; Crystallization ; Crystallography, X-Ray ; Hydrogen Bonding ; Mitochondria/enzymology ; Models, Molecular ; Molecular Motor Proteins/*chemistry/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proton-Motive Force ; Proton-Translocating ATPases/*chemistry/metabolism ; Protons ; Saccharomyces cerevisiae/enzymology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 1995-04-28
    Description: The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement and cyclic averaging. The atomic model was built and refined to a crystallographic R factor of 22.1 percent. The 673-kilodalton protease complex consists of 14 copies of two different subunits, alpha and beta, forming a barrel-shaped structure of four stacked rings. The two inner rings consist of seven beta subunits each, and the two outer rings consist of seven alpha subunits each. A narrow channel controls access to the three inner compartments. The alpha 7 beta 7 beta 7 alpha 7 subunit assembly has 72-point group symmetry. The structures of the alpha and beta subunits are similar, consisting of a core of two antiparallel beta sheets that is flanked by alpha helices on both sides. The binding of a peptide aldehyde inhibitor marks the active site in the central cavity at the amino termini of the beta subunits and suggests a novel proteolytic mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lowe, J -- Stock, D -- Jap, B -- Zwickl, P -- Baumeister, W -- Huber, R -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):533-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Biochemie, Abteilung fur Strukturforschung, Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725097" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Archaeal Proteins ; Binding Sites ; Chaperonin 60/chemistry ; Computer Graphics ; Crystallography, X-Ray ; Cysteine Endopeptidases/*chemistry/metabolism ; Endopeptidases/*chemistry/metabolism ; Fourier Analysis ; Hydrogen Bonding ; Leupeptins/chemistry/metabolism ; *Models, Molecular ; Molecular Sequence Data ; Multienzyme Complexes/*chemistry/metabolism ; Protease Inhibitors/chemistry/metabolism ; Proteasome Endopeptidase Complex ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proteins/metabolism ; Thermoplasma/*enzymology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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