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'Ribulose l' in keywords
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1988 (1)
1980 (1)
1Author    GünterF. Wildner, PrafullachandraV. Sane, Jürgen HenkelRequires cookie*
 Title    The Activation of Ribulose-l,5-bisphosphate Carboxylase-Oxygenase from Spinach by Oxygen Changes of the Enzyme Conformation during Air-Argon Transitions  
 Abstract    The effect of oxygen on ribulose-l,5-bisphosphate carboxylase-oxygenase from spinach was in­ vestigated. Both activities were deactivated by removal of oxygen and reversibly reactivated by oxygenation of the enzyme solution. The change in enzyme activities was accompanied by confor­ mational changes as studied by the use of intrinsic and extrinsic fluorescent probes. The analysis of cysteine sulfhydryl groups accessible to 5,5'-dithiobis-(2-nitrobenzoic acid) re­ vealed that the number of these groups changed with the oxygen concentration. The kinetic of the exposure of eight cysteine residues was similar to the loss of enzyme activities. The modification of these groups with 5,5'-dithiobis-(2-nitrobenzoic acid) caused almost complete loss of both the activities. The enzyme isolated from a photolithotrophic organism, Chromatium vinosum, was not affected by oxygen removal. During air — argon transitions, neither the enzyme conformation nor the num­ ber of accessible sulfhydryl groups changed. 
  Reference    Z. Naturforsch. 35c, 239—248 (1980); received December 12 1979 
  Published    1980 
  Keywords    Ribulose-l, 5-bisphosphate Carboxylase, Ribulose-l, 5-bisphosphate Oxygenase, Enzyme Confor­ mation, Oxygen Effect, Photosynthesis 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0239.pdf 
 Identifier    ZNC-1980-35c-0239 
 Volume    35 
2Author    P. M. Abuja, I. PilzRequires cookie*
 Title    Investigation of Ribulose-1,5-bisphosphate Carboxylase-Oxygenase from Tobacco by Small Angle X-Ray Scattering: A Structural Model for the Enzyme in Solution  
 Abstract    The quaternary structure of ribulose-l,5-bisphosphate carboxylase/oxygenase from tobacco (Nicotiana tabacum) was investigated in solution by means of small angle X-ray scattering. The most important molecular parameters as the radius of gyration (Rg) and the maximum diameter (Dmax) were determined. Both the active and the inactive form of the enzyme were measured at 5 °C and at 20 °C. A more distinct difference in size could be detected between the inactive forms at these two temperatures (Rg = 4.80 nm (5 °C) and 4.68 nm (20 °C)) than between the active forms (Rg = 4.73 nm and 4.69 nm). The maximum diameters were determined to be 13.1 nm for the inactive form at 5 °C and 12.8 nm for the other forms. A model is proposed consisting of eight large and eight small subunits arranged in the way that seems to be typical for this enzyme in higher plants. 
  Reference    Z. Naturforsch. 43c, 373—376 (1988); received December 21 1987/February 15 1988 
  Published    1988 
  Keywords    Small-Angle X-Ray Scattering, Solution Structure, Ribulose-l, 5-bisphosphate Carboxylase/ Oxygenase, Conformational Change, Temperature Effect 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0373.pdf 
 Identifier    ZNC-1988-43c-0373 
 Volume    43