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C H Foyer

Publications and source records attributed to C H Foyer.

47 records · Page 3Linked to original sources
PubMed1990

Relationship between Photosynthetic Electron Transport and Stromal Enzyme Activity in Pea Leaves : Toward an Understanding of the Nature of Photosynthetic Control.

The responses of the quantum efficiencies of photosystem (PS) II and PSI measured in vivo simultaneously with estimations of the activities and activation states of NADP-malate dehydrogenase, chloroplast fructose-1,6-bisphosphatase, and ribulose-1,5-bisphosphate carboxylase were used to study the relationship between electron transport and carbon metabolism. The effects of varying irradiance and CO(2) partial pressure on the relationship between the quantum efficiencies of PSI and II, and the activity of these enzymes shows that the interrelationships vary according to the limitations placed on the system. The relationship between the quantum efficiencies of PSII and PSI was linear in most situations. In response to increasing irradiance, the activity of all three enzymes increased. In the case of NADP-malate dehydrogenase this increase was well correlated with the estimated flux of electrons through PSI and PSII. The other two enzymes showed a more complex relationship with the estimated flux of electrons through both photosystems. These relationships are consistent with the known interactions between these stromal enzymes and the thylakoids. The response to varying CO(2) partial pressure is more complex. The efficiencies of PSI and II declined with decreasing CO(2) partial pressure and the activity of each enzyme varied uniquely. However, there are clear correlations between the activities of the enzymes and the flux of electrons through the photosystems. In contrast to the data obtained under conditions of varying irradiance, there is clear evidence of photosynthetic control of electron transport when the CO(2) concentration is varied.

Journal Article↗
PubMed1989

Coregulation of electron transport and Benson-Calvin cycle activity in isolated spinach chloroplasts: studies on glycerate 3-phosphate reduction.

Glycerate 3-phosphate-dependent O2 evolution was measured in intact chloroplasts in the absence of CO2. At all concentrations of added glycerate 3-phosphate oxygen evolution ceased before stoichiometric amounts of oxygen were evolved. The inhibition of glycerate 3-phosphate-dependent-O2 evolution increased with increasing concentrations of substrate added. A similar response was observed in chloroplasts treated with KCN which inhibits ribulose-1,5-bisphosphate carboxylase-oxygenase. Oxygen uptake via the oxygenase activity of this enzyme is therefore not the cause of the discrepancy in stoichiometry of oxygen release in this system. The addition of NaHCO3 to chloroplasts in which oxygen evolution was inhibited by glycerate 3-phosphate caused an immediate sustained rate of oxygen evolution in the absence of KCN but not with KCN present. Simultaneous measurements of chlorophyll a fluorescence showed that qQ remained oxidized, although net O2 evolution had ceased. As O2 evolution decreased, qE and delta pH increased. Upon the addition of the NaHCO3, QA became more oxidized while delta pH and qE were decreased, suggesting that the inhibition of electron transport at high glycerate 3-phosphate concentrations was mediated by photosynthetic control via delta pH. However, the levels of ATP, ADP, ribulose 1,5-bisphosphate, and Pi concentrations and ATP/ADP ratio. The stromal glycerate 3-phosphate content declined upon illumination until O2 evolution ceased. At this time a constant stromal glycerate 3-phosphate concentration of 8-10 mM was maintained while net import of glycerate 3-phosphate into the stroma had virtually ceased. The stromal triosephosphate content remained at a constant low level throughout but the glycerate 3-phosphate level increased slightly after addition of NaHCO3. The data provided by the measurements of thylakoid reactions and stromal metabolites suggest that photosynthetic electron transport is tightly coupled to the requirements of the stroma for ATP and NADPH. Glycerate 3-phosphate reduction requires much less ATP than the operation of the complete Benson-Calvin cycle since the stoichiometry of ATP and NADPH utilization is reduced to 1:1. We conclude that thylakoid electron flow is not sufficiently flexible to maintain NADPH and ATP production in the ratio of 1:1. This situation will favor overenergization of the thylakoid membrane, increased leakiness of protons, increased electron drainage to O2, and result in progressive inhibition of noncyclic electron flow.

Antimycin A↗
PubMed1989

Limitation of CO(2) Assimilation and Regulation of Benson-Calvin Cycle Activity in Barley Leaves in Response to Changes in Irradiance, Photoinhibition, and Recovery.

The response of the Benson-Calvin cycle to changes in irradiance and photoinhibition was measured in low-light grown barley (Hordeum vulgare) leaves. Upon the transition from the growth irradiance (280 micromoles per square meter per second) to a high photoinhibitory irradiance (1400 micromoles per square meter per second), the CO(2) assimilation rate of the leaves doubled within minutes but high irradiance rapidly caused a reduction in quantum efficiency. Following exposure to high light the activities of NADP-malate dehydrogenase and fructose-1,6-bisphosphatase obtained near maximum values and the activation state of ribulose-1,5-bisphosphate carboxylase increased. The activity of the latter remained constant throughout the period of photoinhibitory irradiance, but the increase in the activities of fructose-1,6-bisphosphatase and NADP-malate dehydrogenase was transient decreasing once more to much lower values. This suggests that immediately following the transition to high light reduction and activation of redox-modulated enzymes occurred, but then the stroma became relatively oxidized as a result of photoinhibition. The leaf contents of glucose 6-phosphate and fructose 6-phosphate increased following exposure to high light but subsequently decreased, suggesting that following photoinhibition sucrose synthesis exceeded the rate of carbon assimilation. The ATP content attained a constant value much higher than that in low light. During photoinhibition the glycerate 3-phosphate content greatly increased while ribulose-1,5-bisphosphate decreased. The fructose-1,6-bisphosphate and triose phosphate contents increased initially and then remained constant. During photoinhibition CO(2) assimilation was not limited by ribulose-1,5-bisphosphate carboxylase activity but rather by the regeneration of the substrate, ribulose-1,5-bisphosphate, related to a restriction on the supply of reducing equivalents.

Journal Article↗
PubMed1988

Regulation of ribulose-1,5-bisphosphate carboxylase activity by the activase system in lysed spinach chloroplasts.

Ribulose-1,5-bisphosphate (RuBP) carboxylase in lysed spinach (Spinacia oleracea L. cv virtuosa) chloroplasts that had been partly inactivated at low CO(2) and Mg(2+) by incubating in darkness with 4 millimolar partially purified RuBP was reactivated by light. If purified RuBP was used to inhibit dark activation of the enzyme, reactivation by light was not observed unless fructose-1,6-bisphosphate, ATP, or ADP plus inorganic phosphate were also added. Presumably, ADP plus inorganic phosphate acted as an ATP-generating system with a requirement for the generation of DeltapH across the thylakoid membrane. When the RuBP obtained from Sigma Chemical Co. was used, light did not reactivate the enzyme. There was no direct correlation between DeltapH and activation. Therefore, thylakoids are required in the ribulose-1,5-bisphosphate carboxylase activase system largely to synthesize ATP. Inactivation of RuBP carboxylase in isolated chloroplasts or in the lysed chloroplast system was not promoted simply by a transition from light to dark conditions but was caused by low CO(2) and Mg(2+).

Journal Article↗
PubMed1987

Evidence for different kinases in thylakoid protein phosphorylation.

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.

Bicarbonates↗
PubMed1986

Oscillations in levels of metabolites from the photosynthetic carbon reduction cycle in spinach leaf disks generated by the transition from air to 5% CO2.

Variations in the endogenous concentrations of leaf metabolites were measured during the transition from steady-state photosynthesis in air to that in 5% CO2, 21% O2. The transition in the CO2 supply to the leaf caused a pronounced oscillation in the overall rate of photosynthesis, as indicated by chlorophyll a fluorescence, which was accompanied by large changes in the levels of metabolites associated with carbon metabolism. A dramatic increase in the ATP concentration occurred immediately following the gas transition and was maximal at the point at which the chlorophyll a fluorescence showed a transient decrease. During the first large fluorescence increase the ATP level rapidly declined. Oscillations in the level of 3-phosphoglycerate were the most pronounced of the photosynthetic metabolites measured. These accompanied the oscillations in chlorophyll a fluorescence which showed an inverse relationship to the oscillations in ATP/ADP ratio. The ribulose 1,5-bisphosphate concentration showed a small increase following the gas transition but subsequently fell much lower, enforced by the high level of CO2 supplied. Less pronounced oscillations in the intracellular concentrations of fructose 1,6-bisphosphate, fructose 6-phosphate, glucose 6-phosphate, and triose phosphate were also observed.

Adenosine Diphosphate↗
PubMed1985

Stromal protein phosphorylation in spinach (Spinacia oleracea) chloroplasts.

When intact spinach chloroplasts were supplied with [32P]Pi, stromal protein phosphorylation was found to occur in the dark. On illumination the thylakoid protein kinase was activated and the amount of label found in thylakoid proteins quickly exceeded that incorporated into stromal protein, such that the latter was found to account for only 10-15% of the total radioactivity bound to chloroplast proteins after 5 min illumination. The rate of phosphorylation of stromal polypeptides was unchanged by light. After SDS/polyacrylamide-gel electrophoresis, more than 15 labelled polypeptides of stromal origin were observed. A polypeptide with an Mr of approx. 70 000 had the highest specific activity of labelling. Both the large and small subunits of the ribulose-1,5-bisphosphate carboxylase were phosphorylated. The level of phosphorylation of stromal protein was increased by CO2 fixation in intact chloroplasts. This increase was not observed in the absence of NaHCO3 or in the presence of the phosphoribulokinase inhibitor DL-glyceraldehyde. These effects appeared to be largely due to changes in the phosphorylation state of the large and small subunits of ribulose-1,5-bisphosphate carboxylase. Studies with the reconstituted chloroplast system showed that the thylakoid protein kinase(s) played no part in the phosphorylation of stromal protein. The rate and level of phosphorylation of stromal protein was unaffected by the activation state of the thylakoid protein kinase and was unchanged when thylakoids were omitted from the reaction medium. The phosphorylation of stromal proteins is therefore catalysed by a discrete soluble protein kinase.

Chloroplasts↗
PubMed1981

Similarity of Ribulose-1,5-bisphosphate Carboxylases of Isogenic Diploid and Tetraploid Ryegrass (Lolium perenne L.) Cultivars.

Partially purified ribulose-1,5-bisphosphate carboxylase (EC 4.1.1.39) was isolated from diploid and tetraploid cultivars of ryegrass (Lolium perenne L.) using two separate methods. The apparent K(m) (CO(2)) values for the enzymes prepared by either method did not differ significantly between diploid and tetraploid when assayed by two separate techniques. The unpurified enzymes from freshly lysed (and fully functional) protoplasts of both diploid and tetraploid cultivars gave virtually identical apparent K(m) (CO(2)) values. There was no indication of large differences in affinity for CO(2) of illuminated intact protoplasts from the two cultivars.

Journal Article↗
PubMed1978

Subcellular localisation and identification of superoxide dismutase in the leaves of higher plants.

1. The subcellular location of superoxide dismutase in the leaves of spinach and other C3 plants has been investigated. 2. Most activity appeared to be located within chloroplasts. These organelles contain a cyanide-sensitive (copper-zinc) superoxide dismutase, most of which is located in the stroma although some is bound to the thylakoids. 3. Intact chloroplast fractions also contain a cyanide-insensitive (manganese) superoxide dismutase, but this activity is located on the outside of the chloroplasts and may be adsorbed onto them during isolation. 4. Leaf mitochondrial fractions contain only a small percentage of total leaf superoxide dismutase activity, but there is more than can be accounted for by contamination with chloroplasts. 5. Mitochondria contain both a cyanide-sensitive dismutase, apparently located in the intermembrane space, and a cyanide-insensitive activity, apparently located in the matrix. 6. The microsomal fraction contains no superoxide dismutase activity.

Chloroplasts↗
PubMed1976

Ascorbic acid, metal ions and the superoxide radical.

1. No evidence could be found for production of the superoxide radical, O2-, during autoxidation of ascorbic acid at alkaline pH values. Indeed, ascorbate may be important in protection against O2- genat-d in vivo. 2. Oxidation of ascorbate at pH 10.2 was stimulated by metal ions. Stimulation by Fe2+ was abolished by superoxide dismutase, probably because of generation of O2-- during reduction of O2 by Fe2+, followed by reaction of O2-- with ascorbate. EDTA changed the mechanism of Fe2+-stimulated ascorbate oxidation. 3. Stimulation of ascorbate oxidation by Cu2+ was also decreased by superoxide dismutase, but this appears to be an artifact, since apoenzyme or bovine serum albumin showed similar effects.

Ascorbic Acid↗