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Respiration in energy-transducing membranes of the thermophilic cyanobacterium Mastigocladus laminosus: II. Oxidative phosphorylation
Authors:Ruedi Frei  Andres Binder  Reinhard Bachofen
Institution:Institute for Plant Biology, University of Zürich, Zollikerstr. 107, CH - 8008 Zürich Switzerland
Abstract:Oxidative phosphorylation was measured in isolated energy-transducing membranes of the thermophilic cyanobacterium Mastigocladus laminosus with NADH-mediated electron transport. This dark phosphorylation was similar to photophosphorylation in its sensitivity to uncouplers and energy-transfer inhibitors. However, photophosphorylation was 20- to 50-times more active than oxidative phosphorylation. The PO ratio of oxidative phosphorylation was about 0.2. Besides oxidative phosphorylation, adenylate kinase- and ADP-Pi exchange activity were measured in the dark. The ADP-Pi exchange reaction was identified as polynucleotide phosphorylase.
Keywords:Cyanobacterium  Oxidative phosphorylation  Respiration  Photophosphorylation  Thermophilic bacterium  (M  laminosus)  Tricine  coupling factor isolated from spinach  DCCD  CCCP  EDTA  ethylenediamine tetraacetic acid  ATP synthetized per two electrons transported  PMS  phenazine methosulphate
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