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  • 1
    Publication Date: 2010-06-26
    Description: The heme-copper oxidases (HCOs) accomplish the key event of aerobic respiration; they couple O2 reduction and transmembrane proton pumping. To gain new insights into the still enigmatic process, we structurally characterized a C-family HCO--essential for the pathogenicity of many bacteria--that differs from the two other HCO families, A and B, that have been structurally analyzed. The x-ray structure of the C-family cbb3 oxidase from Pseudomonas stutzeri at 3.2 angstrom resolution shows an electron supply system different from families A and B. Like family-B HCOs, C HCOs have only one pathway, which conducts protons via an alternative tyrosine-histidine cross-link. Structural differences around hemes b and b3 suggest a different redox-driven proton-pumping mechanism and provide clues to explain the higher activity of family-C HCOs at low oxygen concentrations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Buschmann, Sabine -- Warkentin, Eberhard -- Xie, Hao -- Langer, Julian D -- Ermler, Ulrich -- Michel, Hartmut -- New York, N.Y. -- Science. 2010 Jul 16;329(5989):327-30. doi: 10.1126/science.1187303. Epub 2010 Jun 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Biophysik, Max-von-Laue-Strasse 3, D-60438 Frankfurt/Main, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20576851" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Catalytic Domain ; Crystallography, X-Ray ; Cytoplasm/metabolism ; Electron Transport ; Electron Transport Complex IV/*chemistry/*metabolism ; Heme/chemistry ; Histidine/chemistry ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Oxidation-Reduction ; Oxygen/metabolism ; Periplasm/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proton Pumps/*chemistry/*metabolism ; *Protons ; Pseudomonas stutzeri/*enzymology ; Tyrosine/chemistry
    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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  • 2
    Publication Date: 2006-03-18
    Description: Artificial muscles and electric motors found in autonomous robots and prosthetic limbs are typically battery-powered, which severely restricts the duration of their performance and can necessitate long inactivity during battery recharge. To help solve these problems, we demonstrated two types of artificial muscles that convert the chemical energy of high-energy-density fuels to mechanical energy. The first type stores electrical charge and uses changes in stored charge for mechanical actuation. In contrast with electrically powered electrochemical muscles, only half of the actuator cycle is electrochemical. The second type of fuel-powered muscle provides a demonstrated actuator stroke and power density comparable to those of natural skeletal muscle and generated stresses that are over a hundred times higher.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ebron, Von Howard -- Yang, Zhiwei -- Seyer, Daniel J -- Kozlov, Mikhail E -- Oh, Jiyoung -- Xie, Hui -- Razal, Joselito -- Hall, Lee J -- Ferraris, John P -- Macdiarmid, Alan G -- Baughman, Ray H -- New York, N.Y. -- Science. 2006 Mar 17;311(5767):1580-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and NanoTech Institute, University of Texas at Dallas, Richardson, TX 75083-0688, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16543453" target="_blank"〉PubMed〈/a〉
    Keywords: *Artificial Organs ; Biomechanical Phenomena ; *Biomimetic Materials ; Bionics ; Electric Power Supplies ; Electrochemistry ; *Electrodes ; Hydrogen/chemistry ; Lifting ; *Muscle, Skeletal/physiology ; *Nanotubes, Carbon ; Oxidation-Reduction ; Oxygen/chemistry ; Robotics ; Stress, Mechanical
    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
    Electronic Resource
    Electronic Resource
    Springer
    The European physical journal 21 (1991), S. 163-175 
    ISSN: 1434-6079
    Keywords: 03.65. ; 36.40.+d ; 21.60.-n
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Simulating the one-particle spectra of the infinite-well potential by a model, we study the symmetry and the shell-structure of octupole deformations as well as the possible occurrence of octupole (and quadrupole) instabilities. Among various types of octupole deformations investigated theY 32-type deformation is found to have a strong shell-structure as well as a very interesting symmetry which leads to the occurrence of highly-degenerate single-particle levels. One particle spectra of the octupole-coupled two-level model (withl andl + 3) are analytically studied in the limit of large angular-momentum,l.
    Type of Medium: Electronic Resource
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