Characteristics of pea leaves and their relationships to photosynthetic CO2 exchange in the field

1983 ◽  
Vol 61 (12) ◽  
pp. 3283-3292 ◽  
Author(s):  
J. D. Mahon ◽  
S. L. A. Hobbs ◽  
S. O. Salminen
Keyword(s):  
Direct Determination ◽  
Stomatal Resistance ◽  
Co2 Exchange ◽  
Photosynthetic Performance ◽  
Time Of Day ◽  
Ribulose Bisphosphate Carboxylase ◽  
Ribulose Bisphosphate ◽  
Carboxylase Activity ◽  
Single Experiment ◽  
Bisphosphate Carboxylase

Photosynthetic CO2 exchange rate (CER) was determined in attached leaflets of field-grown peas (Pisum sativum L.) Three populations of genotypes were studied in different field locations and years. In 1 year, CER, leaf characteristics, and meteorological factors were measured in parallel at different times of the day and season. Differences in CER across environments or time of day were related to differences in stomatal resistance; however, changes during the season, which might be of environmental or developmental origin, were not. Genotype ranking for CER was largely independent of measuring time, field location, and year. None of the leaf characters which have been suggested as simple assays for photosynthetic ability (specific leaf weight, chlorophyll content, stomatal resistance) was consistently related to CER over several tests. In the single experiment in which they were determined, ribulose bisphosphate carboxylase activity, leaf soluble protein content, and the difference in CER at 2 and 20 kPa O2 were also not correlated with CER. The O2 effect expressed as a percentage of CER at 2 kPa O2 and the slope of the light response above 50 nE cm−2 s−1 were significantly correlated to CER, but neither is suitable for predicting CER in different genotypes. A significant multiple regression of CER on stomatal resistance, total chlorophyll, and ribulose bisphosphate carboxylase activity suggests that the genetic control of CER may involve several characters. In this case, direct determination of CO2 exchange may be the easiest and most reliable way of assessing genetic differences in photosynthetic performance.

scholarly journals Ribulose 1,5-bisphosphate carboxylase. Effect on the catalytic properties of changing methionine-330 to leucine in the Rhodospirillum rubrum enzyme

1986 ◽  
Vol 235 (3) ◽  
pp. 839-846 ◽  
Author(s):  
B E Terzaghi ◽  
W A Laing ◽  
J T Christeller ◽  
G B Petersen ◽  
D F Hill
Keyword(s):  
Rhodospirillum Rubrum ◽  
Oligonucleotide Primer ◽  
Similar Amount ◽  
Ribulose Bisphosphate Carboxylase ◽  
Ribulose Bisphosphate ◽  
Carboxylase Activity ◽  
Bisphosphate Carboxylase ◽  
Ribulose Bisphosphate Carboxylase Oxygenase ◽  
In The Wild ◽  
The Stability

Oligonucleotide-directed mutagenesis of cloned Rhodospirillum rubrum ribulose bisphosphate carboxylase/oxygenase with a synthetic 13mer oligonucleotide primer was used to effect a change at Met-330 to Leu-330. The resultant enzyme was kinetically examined in some detail and the following changes were found. The Km(CO2) increased from 0.16 to 2.35 mM, the Km(ribulose bisphosphate) increased from 0.05 to 1.40 mM for the carboxylase reaction and by a similar amount for the oxygenase reaction. The Ki(O2) increased from 0.17 to 6.00 mM, but the ratio of carboxylase activity to oxygenase activity was scarcely affected by the change in amino acid. The binding of the transition state analogue 2-carboxyribitol 1,5-bisphosphate was reversible in the mutant and essentially irreversible in the wild type enzyme. Inhibition by fructose bisphosphate, competitive with ribulose bisphosphate, was slightly increased in the mutant enzyme. These data suggest that the change of the residue from methionine to leucine decreases the stability of the enediol reaction intermediate.

scholarly journals Ribulose bisphosphate carboxylase/oxygenase in toluene-permeabilized Rhodospirillum rubrum

1983 ◽  
Vol 212 (1) ◽  
pp. 45-54 ◽  
Author(s):  
I Storrø ◽  
B A McFadden
Keyword(s):  
Rhodospirillum Rubrum ◽  
Decay Rates ◽  
Dual Function ◽  
Co2 Removal ◽  
Ribulose Bisphosphate Carboxylase ◽  
Ribulose Bisphosphate ◽  
Carboxylase Activity ◽  
Bisphosphate Carboxylase ◽  
Ribulose Bisphosphate Carboxylase Oxygenase ◽  
The Stability

Toluene-permeabilized Rhodospirillum rubrum cells were used to study activation of and catalysis by the dual-function enzyme ribulose bisphosphate carboxylase/oxygenase. Incubation with CO2 provided as HCO3-, followed by rapid removal of CO2 at 2 degrees C and subsequent incubation at 30 degrees C before assay, enabled a determination of decay rates of the carboxylase and the oxygenase. Half-times at 30 degrees C with 20 mM-Mg2+ were 10.8 and 3.7 min respectively. Additionally, the concentrations of CO2 required for half-maximal activation were 56 and 72 microM for the oxygenase and the carboxylase respectively. After activation and CO2 removal, inactivation of ribulose bisphosphate oxygenase in the presence of 1 mM- or 20mM-Mn2+ was slower than that with the same concentrations of Co2+ or Mg2+. Only the addition of Mg2+ supported ribulose bisphosphate carboxylase activity, as Mn2+, Co2+ and Ni2+ had no effect. A pH increase after activation in the range 6.8-8.0 decreased the stability of the carboxylase but in the range 7.2-8.0 increased the stability of the oxygenase. With regard to catalysis. Km values for ribulose 1,5-bisphosphate4- were 1.5 and 67 microM for the oxygenase and the carboxylase respectively, and 125 microM for O2. Over a broad range of CO2 concentrations in the activation mixture, the pH optima were 7.8 and 8-9.2 for the carboxylase and the oxygenase respectively. The ratio of specific activities was constant (9:1 for the carboxylase/oxygenase) of ribulose bisphosphate carboxylase/oxygenase in toluene-treated Rsp. rubrum. Below concentrations of 10 microM-CO2 in the activation mixture, this ratio increased.

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