scholarly journals Effect of CO2 Concentration on Carbonic Anhydrase and Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Expression in Pea

1996 ◽  
Vol 112 (2) ◽  
pp. 569-574 ◽  
Author(s):  
N. Majeau ◽  
J. R. Coleman
Keyword(s):  
Carbonic Anhydrase ◽  
Co2 Concentration ◽  
Bisphosphate Carboxylase

Regulation of Carboxylation and Photosynthetic Oscillations During Sun-Shade Acclimation in Helianthus annuus Measured With a Rapid-Response Gas Exchange System

1988 ◽  
Vol 15 (2) ◽  
pp. 239 ◽  
Author(s):  
CB Osmond ◽  
V Oja ◽  
A Laisk
Keyword(s):  
Gas Exchange ◽  
Intercellular Co2 Concentration ◽  
Photosynthetic Apparatus ◽  
Co2 Concentration ◽  
Rapid Response ◽  
Exchange System ◽  
Dynamic Regulation ◽  
Bisphosphate Carboxylase ◽  
Shade Acclimation ◽  
Gas Exchange System

The consequences of acclimation from shade to sun and vice versa for regulated photosynthetic metabolism were examined in H. annuus. A rapid-response gas exchange system was used to assess changes in carboxylation-related parameters (mesophyll conductance, assimilatory charge and CO2 capacity) and to analyse oscillations in CO2 fixation following transfer to high CO2 concentration as a function of intercellular CO2 concentration and light intensity. Data showed a two- to threefold change in all carboxylation-related parameters during acclimation in either direction. Dynamic regulation of carboxylation, indicated by changes in oscillatory response as a function of CO2 concentration at light saturation, remained unchanged, consistent with concerted regulation of ribulose-1,5-bisphosphate carboxylase-oxygenase during acclimation. However, the light dependency of oscillations changed during acclimation from shade to sun, and the range of oscillation was closely tied to the maximum rate of steady-state photosynthesis at CO2 saturation. These data imply that changes in the light-absorbing and electron transport components of the photosynthetic apparatus underlie the shift in regulatory behaviour during acclimation.

scholarly journals A model for the kinetics of activation and catalysis of ribulose 1,5-bisphosphate carboxylase

1976 ◽  
Vol 159 (3) ◽  
pp. 563-570 ◽  
Author(s):  
W A Laing ◽  
J T Christeller
Keyword(s):  
Initial Rate ◽  
Equilibrium Constants ◽  
Co2 Concentration ◽  
Time Dependent ◽  
Enzyme Complex ◽  
Ribulose Bisphosphate Carboxylase ◽  
Ribulose Bisphosphate ◽  
Bisphosphate Carboxylase ◽  
Rate Of Reaction ◽  
Kinetics Of

Further evidence for time-dependent interconversions between active and inactive states of ribulose 1,5-bisphosphate carboxylase is presented. It was found that ribulose bisphosphate oxygenase and ribulose bisphosphate carboxylase could be totally inactivated by excluding CO2 and Mg2+ during dialysis of the enzyme at 4 degrees C. When initially inactive enzyme was assayed, the rate of reaction continually increased with time, and the rate was inversely related to the ribulose bisphosphare concentration. The initial rate of fully activated enzyme showed normal Michaelis-Menten kinetics with respect to ribulose bisphosphate (Km = 10muM). Activation was shown to depend on both CO2 and Mg2+ concentrations, with equilibrium constants for activation of about 100muM and 1 mM respectively. In contrast with activation, catalysis appeared to be independent of Mg2+ concentration, but dependent on CO2 concentration, with a Km(CO2) of about 10muM. By studying activation and de-activation of ribulose bisphosphate carboxylase as a function of CO2 and Mg2+ concentrations, the values of the kinetic constants for these actions have been determined. We propose a model for activation and catalysis of ribulose bisphosphate carboxylase: (see book) where E represents free inactive enzyme; complex in parentheses, activated enzyme; R, ribulose bisphosphate; M, Mg2+; C, CO2; P, the product. We propose that ribulose bisphosphate can bind to both the active and inactive forms of the enzyme, and slow inter-conversion between the two states occurs.

scholarly journals Rubisco proton production can drive the elevation of CO2 within condensates and carboxysomes

2021 ◽  
Vol 118 (18) ◽  
pp. e2014406118
Author(s):  
Benedict M. Long ◽  
Britta Förster ◽  
Sacha B. Pulsford ◽  
G. Dean Price ◽  
Murray R. Badger
Keyword(s):  
Carbonic Anhydrase ◽  
Reaction Diffusion ◽  
Compartment Model ◽  
Low Light ◽  
Bisphosphate Carboxylase ◽  
Proton Production ◽  
Logical Sequence ◽  
Photosynthetic Carbon ◽  
Internal Ph ◽  
Improved Function

Membraneless organelles containing the enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) are a common feature of organisms utilizing CO2 concentrating mechanisms to enhance photosynthetic carbon acquisition. In cyanobacteria and proteobacteria, the Rubisco condensate is encapsulated in a proteinaceous shell, collectively termed a carboxysome, while some algae and hornworts have evolved Rubisco condensates known as pyrenoids. In both cases, CO2 fixation is enhanced compared with the free enzyme. Previous mathematical models have attributed the improved function of carboxysomes to the generation of elevated CO2 within the organelle via a colocalized carbonic anhydrase (CA) and inwardly diffusing HCO3−, which have accumulated in the cytoplasm via dedicated transporters. Here, we present a concept in which we consider the net of two protons produced in every Rubisco carboxylase reaction. We evaluate this in a reaction–diffusion compartment model to investigate functional advantages these protons may provide Rubisco condensates and carboxysomes, prior to the evolution of HCO3− accumulation. Our model highlights that diffusional resistance to reaction species within a condensate allows Rubisco-derived protons to drive the conversion of HCO3− to CO2 via colocalized CA, enhancing both condensate [CO2] and Rubisco rate. Protonation of Rubisco substrate (RuBP) and product (phosphoglycerate) plays an important role in modulating internal pH and CO2 generation. Application of the model to putative evolutionary ancestors, prior to contemporary cellular HCO3− accumulation, revealed photosynthetic enhancements along a logical sequence of advancements, via Rubisco condensation, to fully formed carboxysomes. Our model suggests that evolution of Rubisco condensation could be favored under low CO2 and low light environments.

Distribution of luminal carbonic anhydrase activity along rat inner medullary collecting duct

1991 ◽  
Vol 260 (5) ◽  
pp. F738-F748 ◽  
Author(s):  
S. M. Wall ◽  
M. F. Flessner ◽  
M. A. Knepper
Keyword(s):  
Carbonic Anhydrase ◽  
Collecting Duct ◽  
Co2 Concentration ◽  
Carbonic Anhydrase Activity ◽  
Inner Medullary Collecting Duct ◽  
Proton Source ◽  
Total Ammonia ◽  
Medullary Collecting Duct ◽  
Disequilibrium Ph ◽  
Ammonia Flux

The isolated perfused tubule technique was utilized to determine whether endogenous luminal carbonic anhydrase is present in the initial or terminal parts of the inner medullary collecting duct (IMCD) of the rat. This was accomplished by measuring the luminal disequilibrium pH in the presence of a large luminal proton source created by perfusing the lumen with a solution containing 10 mM NH4Cl. (NH3 efflux causes H+ to be released from NH+4 in the lumen). The disequilibrium pH was calculated by subtracting the equilibrium pH from the measured pH at the end of the tubule lumen. The end-luminal equilibrium pH was calculated from the total CO2 concentration in the collected fluid, as measured by microcalorimetry. The end-luminal pH was determined by measuring the fluorescent signal from the the pH-sensitive dye 2',7'-bis(2-carboxyethyl)-5(6)-carboxyfluorescein (BCECF), which was added to the luminal perfusate in its nonesterified form. In the initial IMCD, there was no measurable disequilibrium pH. With the addition of the carbonic anhydrase inhibitor acetazolamide to the luminal fluid, a significant acidic pH disequilibrium was elicited. In the terminal IMCD under control conditions a statistically significant acidic disequilibrium pH was measured. The disequilibrium was obliterated when exogenous carbonic anhydrase was added to the luminal perfusate. These findings were verified by measuring total ammonia flux by ultramicrofluorometry. The results demonstrate endogenous luminal carbonic anhydrase activity in the initial IMCD but a lack of enzyme activity in the terminal IMCD.

Direct evaluation of acidification by rat testis and epididymis: role of carbonic anhydrase

1990 ◽  
Vol 258 (1) ◽  
pp. E143-E150 ◽  
Author(s):  
C. R. Caflisch ◽  
T. D. DuBose
Keyword(s):  
Carbonic Anhydrase ◽  
Co2 Concentration ◽  
Seminiferous Tubules ◽  
Direct Evaluation ◽  
Rat Testis ◽  
Arterial Blood ◽  
Co2 Concentrations ◽  
Primary Fluid ◽  
Cauda Epididymidis

The present experiments have employed microelectrode techniques (pH and PCO2) and microcalorimetry (total CO2 concentration) to define parameters of acidification in specific structures of the rat testis and epididymis during control conditions and after administration of the carbonic anhydrase inhibitor acetazolamide (20 or 50 mg/kg). Values for in situ pH during control conditions in seminiferous tubules (ST; 6.96 +/- 0.01), proximal caput (PCP; 6.62 +/- 0.01), middle caput (MCP; 6.59 +/- 0.01), middle corpus (MCR; 7.10 +/- 0.02), and proximal cauda epididymidis (PCD; 6.85 +/- 0.01) were significantly more acidic than in testicular artery (TA; 7.36 +/- 0.01) or systemic arterial blood (SAB; 7.40 +/- 0.01) and did not change significantly after acetazolamide. In situ partial pressure of CO2 (PCO2) in TA (52.2 +/- 0.6 mmHg), ST (52.3 +/- 0.4 mmHg), PCP (52.9 +/- 0.4 mmHg), MCP (53.0 +/- 0.7 mmHg), MCR (53.4 +/- 0.4 mmHg), and PCD (52.4 +/- 0.4 mmHg) were indistinguishable from each other, but all values were significantly higher than SAB PCO2 (39.2 +/- 0.5 mmHg). Acetazolamide increased in situ PCO2 significantly in all structures except the MCR. The total CO2 concentration in normal ST fluid (10.7 +/- 0.5 mM) was significantly higher than in "primary" fluid (6.9 +/- 0.3 mM), and both values were well below TA (26.9 +/- 1.3 mM) or SAB (24.6 +/- 0.4 mM) total CO2 concentrations. In the epididymis, total CO2 concentrations were indistinguishable and not different from the value in primary fluid.(ABSTRACT TRUNCATED AT 250 WORDS)

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