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
Partial sequence of ribulose-1,5-bisphosphate carboxylase/oxygenase and the phylogeny ofProchloronandProchlorococcus(Prochlorales)
β Scribed by Atsuhiro Shimada; Satoru Kanai; Tadashi Maruyama
- Publisher
- Springer
- Year
- 1995
- Tongue
- English
- Weight
- 661 KB
- Volume
- 40
- Category
- Article
- ISSN
- 0022-2844
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β¦ Synopsis
The prochlorophytes, oxygenic photosynthetic prokaryotes having no phycobiliprotein but possessing chlorophylls a and b, have been proposed to have a common ancestry with green chloroplasts, yet this is still controversal. We report here that partial sequence comparisons of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase, including sequence data from two prochlorophytes, Prochlorococcus and Prochloron, indicate that Prochlorococcus is more closely related to a photosynthetic bacterium, Chromatium vinosum ('/-purple bacteria), than to cyanobacteria, while Prochloron is closely related to the prochlorophyte Prochlorothrix and to cyanobacteria. The molecular phylogenetic tree indicates that a common ancestor of Prochlorococcus and ?-purple bacteria branched off from the land plant lineage earlier than Prochloron, Prochlorothrix, and cyanobacteria.
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Complete stoichiometry of the reaction catalyzed by ribulose l$bisphosphate (RuBP) oxygenase from spinach and Rhodospirillum rubrum has been determined. Before initiation and after termination, RuBP has been measured either by release of equimolar orthophosphate at 25'C in the presence of 1 N NaOH o