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'ATP Synthase' in keywords Facet   section ZfN Section C  [X]
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1988 (1)
1987 (1)
1984 (1)
1Author    EgbertJ. Boekema, Günter Schmidt, Peter Gräber, JanA. BerdenRequires cookie*
 Title    Structure of the ATP-Synthase from Chloroplasts and Mitochondria Studied by Electron Microscopy  
 Abstract    The structure of the ATP-synthase, F 0 F,, from spinach chloroplasts and beef heart mitochon-dria has been investigated by electron microscopy with negatively stained specimens. The deter-gent-solubilized ATP-synthase forms string-like structures in which the F 0 parts are aggregated. In most cases, the F, parts are arranged at alternating sides along the string. The F 0 part has an approximate cylindrical shape with heights of 8.3 and 8.9 nm and diameters of 6.2 and 6.4 nm for the chloroplast and mitochondrial enzyme, respectively. The F, parts are disk-like structures with a diameter of about 11.5 nm and a height of about 8.5 nm. The F, parts are attached to the strings, composed of F n parts, in most cases, with their smallest dimension parallel to the strings. The stalk connecting F 0 and F, has a length of 3.7 nm and 4.3 nm and a diameter of 2.7 nm and 4.3 nm for the chloroplast and mitochondrial enzyme, respectively. 
  Reference    Z. Naturforsch. 43c, 219—225 (1988); received December 1 1987 
  Published    1988 
  Keywords    ATP-Synthase, Enzyme Structure, Electron Microscopy 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0219.pdf 
 Identifier    ZNC-1988-43c-0219 
 Volume    43 
2Author    G. Ünter Schmidt, PeterG. RäberRequires cookie*
 Title    The Rate of ATP Hydrolysis Catalyzed by Reconstituted CF0F i-Liposomes  
 Abstract    The conditions for optimal rates of ATP hydrolysis catalyzed by the chloroplast ATP-synthase (A T P ase), CFoF,, after isolation and reconstitution into asolectin liposomes have been investi­ gated. The rate of ATP hydrolysis was m easured either after oxidation of CF0F, (by incubation with iodosobenzoate) or after reduction of CFoF, (by incubation with dithiothreitol). In both cases a rate of about 1 -2 A TP (CF0F i-s)" ' was observed under uncoupled conditions. If the pro-teoliposom es are first energized by an acid-base transition and a K"/valinomycin diffusion po ten ­ tial, the uncoupled rate of A TP hydrolysis is about 1 -2 A TP (CFnF, -s) '1 for the oxidized enzyme and about 20 for the reduced species. This rate is about a factor 2 smaller than that observed in chloroolasts under the same conditions. 
  Reference    Z. Naturforsch. 42c, 231 (1987); received O ctober 17 1986 
  Published    1987 
  Keywords    A TP Hydrolysis, ATP Synthase, A TPase, Reconstitution, CF0F, Liposomes 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-0231.pdf 
 Identifier    ZNC-1987-42c-0231 
 Volume    42 
3Author    Peter BögerRequires cookie*
 Title    Multiple Modes of Action of Diphenyl Ethers  
  Reference    Z. Naturforsch. 39c, 468 (1984); received N ovem ber 15 1983 
  Published    1984 
  Keywords    Herbicides, Electron Transport, Peroxidation, N itro/N on-nitro-d iphenyl Ethers, Carotenogenesis, m-Phenoxybenzamides, ATP-Synthase, Stress Response 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0468.pdf 
 Identifier    ZNC-1984-39c-0468 
 Volume    39