Showing papers by "Christine H. Foyer published in 1987"
Journal Article•
TL;DR: In this article, a derivation de Trop plein is branchee sur la voie de synthese du saccharose, impliquant l'hydrolyse du glucose et fructose, suivie de la phosphotylation de ces sucres en hexoses phosphates.
102 citations
TL;DR: The data presented here show that there are multiple sites of flux control exerted by low stromal Pi in the chloroplast, consistent with the hypothesis that Pi limitation results in decreased ATP production by the thylakoid ATP synthase.
55 citations
TL;DR: Physiological concentrations of glycerate 3-phosphate were found to inhibit carboxylation severely, particularly at rate-limiting ribulose 1,5-bisph phosphate concentrations.
24 citations
TL;DR: The presence of ribulose-1,5-bisphosphate carboxylase significantly altered the values obtained for apparent K m for inorganic phosphate and ADP of coupled electron transport in washed thylakoids and in ‘leaky’ chloroplasts.
12 citations
TL;DR: In this paper, the authors showed that the protein kinase that phosphorylates LHCP is distinct from that which phosphoryls the 9 kDa polypeptide.
Abstract: Thylakoid protein phosphorylation was facilitated in darkness by using the ferredoxin-NADPH system. CoCl2 and DBMIB (2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone) were potent inhibitors of LHCP (light-harvesting chlorophyll-binding protein) phosphorylation, but 3-(3,4-dichlorophenyl)-1,1-dimethyl-urea and atrazine had no significant effect. Differential effects on phosphorylation of the 9 kDa polypeptide and LHCP were observed in darkness with DBMIB and certain other inhibitors specific for Photosystem-II electron transport. Similarly, during illumination of intact chloroplasts or of the reconstituted chloroplast system, a differential action of bicarbonate was observed on the relative phosphorylation of the two proteins. The degree of phosphorylation of the 9 kDa polypeptide was increased in the presence of bicarbonate compared with its absence, whereas that of LHCP was relatively unchanged. Changes in the degree of phosphorylation of the 32 kDa polypeptide in these experiments did not correlate consistently with changes in phosphorylation of either LHCP or the 9 kDa polypeptide, although changes in the 32 kDa polypeptide more often paralleled phosphorylation of the 9 kDa polypeptide rather than the phosphorylation of LHCP. These observations suggest that the protein kinase that phosphorylates LHCP is distinct from that which phosphorylates the 9 kDa polypeptide.
2 citations
01 Jan 1987
TL;DR: The following experiments demonstrate that the high binding capacity of this protein has significant repercussions not only on the activity of the enzyme itself but also on other important reactions of photosynthesis.
Abstract: The chloroplast stroma contains a high concentration of the enzyme ribulose-1,5-bisphosphate(RuBP)carboxylase (1). The measured concentration of this protein is 0.4–0.5 mM which is equivalent to 3–4 mM active sites (2) although the theoretical maximum concentration is 1.2 mM carboxylase protein (or 9 mM active sites, 3,4). The following experiments demonstrate that the high binding capacity of this protein has significant repercussions not only on the activity of the enzyme itself but also on other important reactions of photosynthesis.
1 citations