A Study on Oxygen Evolution and on the S-State Distribution in Thylakoid Preparations of the Filamentous Blue-Green Alga Oscillatoria chalybea

1983 ◽  
Vol 38 (9-10) ◽  
pp. 778-792 ◽  
Author(s):  
Klaus P. Bader ◽  
Pierre Thibault ◽  
Georg H. Schmid

When thylakoid preparations of the filamentous blue-green alga Oscillatoria chalybea are exposed to short (2 or 8 μs) saturating light flashes, the oxygen evolution pattern can be distinguished in several respects from the one usually observed in Chlorella. Thus, it appears that a substantial electrochemical signal is already seen under the first flash with maximal flash yield always occurring under the fourth flash. This refers to dark adapted preparations (up to 60 min). Fitting of such an experimental sequence in the 4-state Kok model yields an S-state population consisting of 36-41% S0, 40-49% S1, 1-10% S2 and up to 13% S3. No abnormality under the first flash is seen in such preparations. Characteristic for sequences with Oscillatoria prepara­tions is a high level of misses which are in the region of 25 per cent, whereas double hits do not seem to play a substantial role in the damping of such sequences. The existence of metastable S3, anyway inconsistent with the coherent Kok model, is not confirmed by mass spectrometry. No 18O2 seems to be evolved under the first flash from Oscillatoria thylakoids suspended in 50% H218O. although, when judged from the absolute amperometric signal amplitude, mass spectrometric detection of O2 should have been possible. With the same method we are fully able to detect 18O2 under the second flash in Chlorella vulgaris. In Chlorella this is true for experimental conditions in which the amperometric signal amplitude under the second flash is even smaller than those under the first or second flash in Oscillatoria. The attempt to correlate the amperometrie signal observed under the first flash with a photoinhibition of respiration in our pro­karyotic organism was not successful. However, the attempt to incorporate the phenomenon in the coherent Kok model shows that the Oscillatoria sequence fully resembles those with Chlorella, if the first flash signal and 40-50% of the signal observed under the second flash is simply removed from the sequence. The remaining sequence exhibits the usual properties known from Chlorella or higher plant chloroplasts. If one assumes contribution of the reduced state S-1 to the dark population of S-states, a fit in the five rank Kok model yields correct adjustments with a S-state distribution of 6-20% S-1, 31-40% S0, 49-54% S1, 0% S2 and 0% S3 which would be fully consistent with the Kok model and corresponds to the distribution observed with Chlorella or higher plant chloroplasts. The question what the first electrochemical signal is due to remains unanswered.

1996 ◽  
Vol 51 (11-12) ◽  
pp. 823-832 ◽  
Author(s):  
K Burda ◽  
P He ◽  
K. P Bader ◽  
G. H Schmid

Abstract Five characteristic discontinuities of the pattern of oxygen evolution have been detected for the filamentous cyanobacterium Oscillatoria chalybea in the temperature range of 0°C to 30°C. The temperatures at which these discontinuities occur are: ≈ 5°C, ≈ 11°C, ≈ 15°C, ≈ 21°C and ≈ 25°C. The calculated initial 5-S state distribution, the miss parameter and the fraction of the fast transition S3 → S0+ O2 are affected. The discontinuities are observed at the same transition temperature also for Chlorella kessleri hence are not specific for the cyanobacterium. Based on these studies it is concluded that the not vanishing oxygen signal under the first flash of a flash train in Oscillatoria cannot have its origin in interactions between oxygen-evolving complexes. A decrease of temperature should slow down the expected charge exchanges, improve the oscillations, thus reduce or lower the first two oxygen amplitudes of the oscillatoria pattern. Lowering of the temperautres improves the oscillations but does not lower the first O2 signal of the pattern.


1965 ◽  
Vol 20 (8) ◽  
pp. 802-805 ◽  
Author(s):  
Wilhelm Menke

Thylakoids from chloroplasts of Antirrhinum majus and of the blue-green alga Oscillatoria chalybea form folds during the drying on support films. Under favourable conditions, negative staining with uranylacetate gives electron micrographs of these folds which correspond to crosssections of thylakoids. In these preparations the thylakoid membrane seems to consist of a monolayer of particles. These are insoluble in organic solvents. The center to center distance of the particles approximately agrees with the roentgenographically determined center to center distance of the protein particles in the thylakoid membrane. It was not possible to demonstrate lipids in the thylakoid membrane. Because of the background structure of the support film, electron micrographs gave no unequivocal results concerning the structure of the protein layer in surface view.


1979 ◽  
Vol 34 (12) ◽  
pp. 1218-1221 ◽  
Author(s):  
Ursula Lehmann-Kirk ◽  
Klaus P. Bader ◽  
Georg H. Schmid ◽  
Alfons Radunz

An antiserum to synthetic Zeaxanthin inhibits photosynthetic electron transport on the oxygen-evolving side of photosystem II in tobacco chloroplasts and thylakoids of the filamentous blue-green alga Oscillatoria chalybea. The inhibition site lies for both species between the site of electron donation of water or tetramethyl benzidine and that of diphenyl carbazide or manganese II ions. Typical photosystem I reactions are not impaired by the antiserum. The effect of the antiserum concerning the inhibition site is practically identical to that of the earlier described antiserum to violaxanthin. However, the degree of inhibition seems to be generally somewhat lower with the antiserum to Zeaxanthin, than with that to violaxanthin which hints at a lesser accessibility of zeaxanthin, in the tylakoid membrane in comparison to violaxanthin. In the course of these investigations new evidence was obtained that the oxygen-evolving side of the electron transport scheme is differently organized in Oscillatoria chalybea when compared to tobacco chloroplasts. Thus, the silicomolybdate reduction with water as the electron donor is sen­sitive to DCMU in these algae.


1974 ◽  
Vol 20 (12) ◽  
pp. 1633-1637 ◽  
Author(s):  
J. R. Gallon ◽  
T. A. LaRue ◽  
W. G. W. Kurz

In a young culture, photosynthetic-oxygen evolution by Gloeocapsa is at a low level while nitrogenase activity is at its greatest. When the culture ages, there is a rapid increase in photosynthetic pigments and oxygen evolution, and nitrogenase activity decreases. The temporal separation of nitrogen fixation and photosynthesis may serve to protect nitrogenase from oxygen denaturation.


1998 ◽  
Vol 53 (1-2) ◽  
pp. 39-48 ◽  
Author(s):  
E. K. Nénonéné ◽  
M. Méthot ◽  
M. Fragata

Abstract Phosphatidylglycerol (PG) is an anionic lipid of the thylakoid membrane of higher plant chloroplasts. PG was shown previously to stimulate the evolution of oxygen in intact pho­tosystem II (PSII) membranes [Fragata, M., Strzałka, K. and Nénonéné, E. K. (1991) J. Photochem. Photobiol. B: Biol 11, 329-342], In this work, a study was undertaken of the effect of MgCl2 and PG on the CaCl2-mediated recovery of oxygen evolution in a PSII complex depleted of the extrinsic proteins (EP) of molecular masses 17 kDa (EP17) and 24 kDa (EP24), hereunder designated d17.24PSII. This molecular system is structurally close to the PSII core complex of cyanobacteria and is therefore useful in the comparative analysis of PSII-PG relationships in cyanobacteria and the higher plants. This work reveals a new aspect of the thylakoid lipids role in the PSII function, namely the PG effect on intact PSII is observed as well in d17.24PSII. The results show that phosphatidylglycerol has the ability to compensate for the loss of EP17 and EP24 in the PSII complex. That is, PG restores the oxygen evolution in d17.24PSII incubated in the presence of MgCl2 and/or CaCl2 to the levels observed in native PSII. Moreover, the site of H2O degradation in d17.24PSII, including most probably the pool of calcium and chloride ions, would seem to be protected by phosphatidyl­glycerol. This suggests that one of the docking sites of PG in the PSII complex is near EP24, inasmuch as this extrinsic protein participates in the regulation of the affinity of the calcium and chloride ions to the water oxidation site. Furthermore, taking into account that in d17.24PSII the PSII core complex is directly exposed to PG, then the phospholipid effect reported here indicates that phosphatidylglycerol might be a functional effector and mem­brane anchor of the D1 protein in the PSII core complex as was shown recently in the cyanobacterium Oscillatoria chalybea [Kruse, O. and Schmid, G. H. (1995) Z. Naturforsch. 50c, 380-390],


Author(s):  
L. P. Hardie ◽  
D. L. Balkwill ◽  
S. E. Stevens

Agmenellum quadruplicatum is a unicellular, non-nitrogen-fixing, marine cyanobacterium (blue-green alga). The ultrastructure of this organism, when grown in the laboratory with all necessary nutrients, has been characterized thoroughly. In contrast, little is known of its ultrastructure in the specific nutrient-limiting conditions typical of its natural habitat. Iron is one of the nutrients likely to limit this organism in such natural environments. It is also of great importance metabolically, being required for both photosynthesis and assimilation of nitrate. The purpose of this study was to assess the effects (if any) of iron limitation on the ultrastructure of A. quadruplicatum. It was part of a broader endeavor to elucidate the ultrastructure of cyanobacteria in natural systemsActively growing cells were placed in a growth medium containing 1% of its usual iron. The cultures were then sampled periodically for 10 days and prepared for thin sectioning TEM to assess the effects of iron limitation.


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