S03--inhibits the activity of ribulose-l,5-diphosphate carboxylase in isolated spinach chloroplasts. It shows a non-competitive inhibition pattern with respect to ribulose-l,5-diphosphate and Mg++ but a competitive one with respect to I-ICOa-. The Ki-values are 14 mM S03--and 9.5 mM SOa--respectivel
Activation of ribulose-1,5-bisphosphate carboxylase by chloroplast metabolites in a reconstituted spinach chloroplast system
โ Scribed by Klaus J. Lendzian
- Publisher
- Springer-Verlag
- Year
- 1978
- Tongue
- English
- Weight
- 566 KB
- Volume
- 143
- Category
- Article
- ISSN
- 0032-0935
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โฆ Synopsis
In a preparation of soluble components from isolated spinach (Spinecia oleracea L.) chloroplasts, the activity of ribulose-l,5-bisphosphate carboxylase (EC 4.1.1.39) is strongly increased by 6-phosphogluconate or by NADPH at pH 8.0. When the thylakoid system is added to these soluble components (reconstituted chloroplast system) plus ferredoxin, the carboxylase is even more strongly activated in the light. This "light" activation appears to be due to reduction of endogenous NADP + by electrons from the light reactions transferred via ferredoxin, since NADPH alone can activate the purified enzyme in the dark while reduced ferredoxin does not. The regulatory properties of the enzyme in the reconstituted chloroplast system are compared with those of the isolated enzyme, and their possible physiologic significance is discussed.
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