The substrate specificity factor, VcKo/ V o Kc, of spinach (Spinacia oleracea L.) ribulose 1,5-bisphosphate carboxylase/oxygenase was determined at ribulosebisphosphate concentrations between 0.63 and 200 gM, at pH values between 7.4 and 8.9, and at temperatures in the range of 5 ~ C to 40 ~ C. The
EPR studies of ribulose-1,5-bisphosphate carboxylase/oxygenase activated With Cu2+
✍ Scribed by Stenbjörn Styring; Rolf Braändén; Thomas Nilsson
- Publisher
- Elsevier Science
- Year
- 1983
- Tongue
- English
- Weight
- 200 KB
- Volume
- 79
- Category
- Article
- ISSN
- 0020-1693
No coin nor oath required. For personal study only.
✦ Synopsis
NAD from the adsorbent loaded by Cu'+, Cd'+, Zn2+ (purification factor subsequently -15, 20, 17, yield -56-68%) but not Ni2+, Mn2+ (yield 2.2 and 15.8%) or Co'+, Fe3+ (not eluted). This study supports the idea that the interaction of such metal ions as Cu2+ and Zn2+ (Cd") with LRY chromophore (in contrast to the metal ions Mn2+ and Ni2+) stabilizes a particular conformation of dye that is sterically acceptable to the NAD-binding site in ADH.
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The structure of spinach ribulose 1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39) has been investigated by tilted-view electron microscopy of negatively stained monolayer crystals and image processing. The structure determined consists of a cylinder of octagonal cross-section with a large centr
Ribulose 1,5-bisphosphate carboxylase (EC.4.1.1.39) has been obtained from Nicotiana tabacum leaf homogenates with specific activites from 0.5 to 0.8 µmol CO2 fixed (mg protein min)(-1). These activities are reconciled with much lower, previously reported activities. The results suggest that if the
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