Go toArchive
Browse byFacets
Bookbag ( 0 )
'Ferredoxin' in keywords Facet   Publication Year 1978  [X]
Results  3 Items
Sorted by   
Publication Year
1Author    R. G. Binder, B. R. SelmanRequires cookie*
 Title    Ferredoxin Catalyzed Cyclic Photophosphorylation: Reversal of Dibromothymoquinone Inhibition by N ,N ,N ',N '-T etram ethyl- /j-phenylenediamine  
 Abstract    Conditions for washed, spinach thylakoid membranes to catalyze cyclic phosphorylation using ferredoxin as the cofactor for electron transfer have been re-examined. It was found necessary to ''redox poise" the system; however, the best method to accomplish the poising seemed to be the use of a reductant (glucose-6-phosphate) and not by optimizing the rate of phosphorylation with 3-(3,4-dichlorophenyl)-1,1-dimethyl urea (DCMU). Under these conditions, ferredoxin catalyzed cyclic phosphorylation was found to be sensitive to the inhibitors antimycin A and dibromothymo­ quinone (DBM IB). The inhibition of ferredoxin catalyzed cyclic phosphorylation by DBMIB, but not by antimycin A, was completely reversed by N, N, N', N'-tetramethyl-p-phenylenediamine (TM PD). These data are taken as further support for the function of plastoquinone in ferredoxin catalyzed cyclic phosphorylation. The effect of TMPD in reversing the DBMIB inhibition is inter­ preted as the formation of a TMPD bypass on the internal side of the thylakoid membrane around the DBMIB site of inhibition. 
  Reference    Z. Naturforsch. 33c, 261—265 (1978); received November 22 1977 
  Published    1978 
  Keywords    Cyclic Phosphorylation, Chloroplasts, Ferredoxin, Dibromothymoquinone, Phenylenediamine, Photosynthesis 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0261.pdf 
 Identifier    ZNC-1978-33c-0261 
 Volume    33 
2Author    R. Thauer, H. Schirrmacher, W. Schymanski, P. SchönheitRequires cookie*
 Title    A Rapid Procedure for the Purification of Ferredoxin from Spinach Using Polyethyleneimine  
 Abstract    A rapid procedure for the purification of ferredoxin from spinach is described, which is based on the finding that ferredoxins can be precipitated with polyethyleneimines from acetone containing solutions. The ferredoxin was obtained in high yields (25 — 35 mg/kg spinach) and high purity (A 420/ A 27S= O . 4 7) within less than 8 hours. 
  Reference    Z. Naturforsch. 33c, 495—497 (1978); received M ay 17 1978 
  Published    1978 
  Keywords    Ferredoxin, Iron-Sulfur Proteins, Spinach, Photosynthesis, Polyethyleneimine 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0495.pdf 
 Identifier    ZNC-1978-33c-0495 
 Volume    33 
3Author    VickiD. Breazeale, BobB. Buchanan, RicardoA. WolosiukRequires cookie*
 Title    Chloroplast Sedoheptulose 1,7-Bisphosphatase: Evidence for Regulation by the Ferredoxin/Thioredoxin System  
 Abstract    1. A substrate-specific sedoheptulose-l,7-bisphosphatase has been found in chloroplasts and separated from its fructose-1,6-bisphosphatase counterpart. Experiments with antibodies indicate that the two enzymes are structurally different. 2. Activity of the sedoheptulose-l,7-bisphosphatase enzyme was dependent on M g i+ and a reductant. The most effective reductant tested was thioredoxin that was reduced either photochemi-cally via ferredoxin with chloroplasts or chemically with dithiothreitol. Dithiothreitol added alone also activated the enzyme, but reduced glutathione or 2-mercaptoethanol did not. The thioredoxin-activated enzyme was deactivated by oxidized glutathione. 3. The results suggest that the new substrate-specific sedoheptulose-l,7-bisphosphatase depends on light for activity and resembles certain other regulatory enzymes of the reductive pentose phos­ phate cycle in its mode of regulation. 
  Reference    Z. Naturforsch. 33c, 521 (1978); received M ay 16 1978 
  Published    1978 
  Keywords    Sed-P2ase, Ferredoxin, Thioredoxin, Enzyme Regulation 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0521.pdf 
 Identifier    ZNC-1978-33c-0521 
 Volume    33