scholarly journals Cooperative binding of oxygen to the water-splitting enzyme in the filamentous cyanobacterium Oscillatoria chalybea

2000 ◽  
Vol 1456 (2-3) ◽  
pp. 108-120 ◽  
Author(s):  
Klaus P. Bader ◽  
Georg H. Schmid
Keyword(s):  
Water Splitting ◽  
Cooperative Binding ◽  
Filamentous Cyanobacterium ◽  
Oscillatoria Chalybea

A Study on the Life Time of the S3-State in the Filamentous Cyanobacterium Oscillatoria chalybea

1994 ◽  
Vol 49 (1-2) ◽  
pp. 108-114 ◽  
Author(s):  
G. H. Schmid ◽  
K. P. Bader ◽  
R. Schulder
Keyword(s):  
Steady State ◽  
Molecular Oxygen ◽  
Life Time ◽  
State System ◽  
Filamentous Cyanobacterium ◽  
Entire System ◽  
Higher Plant ◽  
Oscillatoria Chalybea ◽  
S States ◽  
Reduced State

In the filamentous cyanobacterium Oscillatoria chalybea deactivation of the S-states starting from steady-state conditions in which S0 = S1 = S2 = S3 = 25% reveals that S3 deactivates to a finite level of approx. 10%. This level is reached under normal conditions between 10-15 seconds. This quasi metastable S3 meets all requirements for S3 in that one flash eliminates this redox conditions to give S4 and therewith molecular oxygen. An analysis of the cyanobacterial S-state system in the 5-state Kok model shows that the S-state population in the dark adapted sample contains no contribution from S-1 or a more reduced condition which under normal conditions is the case for Chlorella or higher plant chloroplasts. Hence under standard conditions, the Oscillatoria condition is a pure Kok-4-condition in which S0 is the most reduced state. Under these conditions S2 seems to deactivate to S1 and S3 to S2 and to a smaller extent to S0. In the presence of the ADRY-reagent Ant-2-p (2-(3-chloro-4-trifluoromethyl)- anilino-3,5-dinitrothiophene) introduced by Renger (Biochim. Biophys. Acta 256,428,1972), which is supposed to specifically act on the S3-state (and thereby on S2), not only the deactivation kinetic of S3 (and S2) is accelerated (hence the life time of the S3-state is shortened), but also the level of metastable S3 becomes practically zero. An analysis of the deactivation pattern shows that the agent changes the mode of deactivation of the entire system. Thus, it is seen that after deactivation of a sample in presence of this agent the dark population of S-states contains the more reduced redox condition S-1 It looks as if in this condition S2 deactivates not only to S1 but also to an appreciable extent by two steps to S-1 Another agent ABDAC (alkyl-benzyl-dimethyl-ammoniumchloride) seems to lengthen the lifetime of the S2 and S3 condition in this cyanobacterium by apparently acting on the membrane condition.

Phosphatidylglycerol and ß-Carotene Bound onto the D 1-Core Peptide of Photosystem II in the Filamentous Cyanobacterium

1994 ◽  
Vol 49 (1-2) ◽  
pp. 115-124 ◽  
Author(s):  
O. Kruse ◽  
A. Radunz ◽  
G. H. Schmid
Keyword(s):  
Fatty Acid ◽  
Photosystem Ii ◽  
Gel Electrophoresis ◽  
Lipid Analysis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Acid Mixture ◽  
Hexadecenoic Acid ◽  
Filamentous Cyanobacterium ◽  
Intact Cells ◽  
Oscillatoria Chalybea

Photosystem II-particles from the cyanobacterium Oscillatoria chalybea were isolated by fractionating centrifugation. Purification of these particles was achieved by a 22 hours centrifugation over a linear sucrose density gradient at 217.500xg. The obtained particle fraction exhibited an oxygen evolution activity which corresponded to three times the rate of intact cells and to five times the rate of intact thylakoids. The chlorophyll protein ratio was 1:10 and the ratio manganese/chlorophyll 1:34. SDS-polyacrylamide gel electrophoresis showed that the photosystem Il-fraction is composed of the core peptides D1 and D2, the chlorophyll-binding peptides CP 43 and CP 47, the extrinsic 33 kDa peptide (manganese stabilizing peptide, MSP) and phycobiliproteins with molecular masses between 16 to 20 kDa. Cyt b559 was not detected in our gel electrophoresis assay. Part of the peptides of the 30 kDa-region (D1, D2, MSP) occurred as aggregates with a molecular mass of 60 to 66 kDa. The D 1-peptide was isolated from the PS Il-preparation by SDS-gel electrophoresis. The intrinisic peptide reacts in the Western blot procedure with the antiserum to phosphatidylglycerol and with the antiserum to β-carotene. Incubation of the peptide with the antisera to monogalactosyldiglyceride, sulfoquinovosyldiglyceride and zeaxanthine resulted negatively. The binding of phosphatidylglycerol onto the D 1-peptide was confirmed by lipid analysis in HPLC and fatty acid analysis by gas chromatography. Only this lipid, respectively the typical fatty acid mixture of this lipid was detected. The lipid is characterized by the fact that the hexadecenoic acid does not exhibit trans-configuration, as is true for phosphatidylglycerol of higher plants and algae, but occurs in cis-configuration. With the antibody being directed towards the glycerol-phosphate residue and not towards the fatty acids, it can be concluded from the reaction of the antibodies with the bound lipid that the lipid is bound to the peptide via the fatty acid. The negatively charged phosphatidylglycerol increases the hydrophobicity of the peptide and leads to a negatively charged surface favouring binding of cations like calcium and magnesium. The fact that incubation of this PS Il-fraction with phospholipase inhibits photosynthetic activity by 25% which can be fully restored by addition of phosphatidylglycerol, shows that bound phosphatidylglycerol has a functional role.

Temperature Dependence of the O2-Oscillation Pattern in the Filamentous Cyanobacterium Oscillatoria chalybea and in Chlorella kessleri

1996 ◽  
Vol 51 (11-12) ◽  
pp. 823-832 ◽  
Author(s):  
K Burda ◽  
P He ◽  
K. P Bader ◽  
G. H Schmid
Keyword(s):  
Transition Temperature ◽  
Temperature Dependence ◽  
Oxygen Evolution ◽  
Filamentous Cyanobacterium ◽  
State Distribution ◽  
Oscillation Pattern ◽  
Chlorella Kessleri ◽  
Temperature Range ◽  
Oscillatoria Chalybea ◽  
Oxygen Evolving

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.

Mass Spectrometric Analysis of N2-Formation Induced by the Oxidation of Hydrazine and Hydroxylamine in Flash Illuminated Thylakoid Preparations of the Filamentous Cyanobacterium Oscillatoria chalybea

1991 ◽  
Vol 46 (7-8) ◽  
pp. 629-634 ◽  
Author(s):  
P. He ◽  
K. P. Bader ◽  
G . H. Schmid
Keyword(s):  
Mass Spectrometry ◽  
Photosystem Ii ◽  
Oxygen Uptake ◽  
Mass Spectrometric ◽  
Spectrometric Analysis ◽  
Filamentous Cyanobacterium ◽  
High Concentration ◽  
Single Turnover ◽  
Oscillatoria Chalybea ◽  
Light Flashes

In tobacco chloroplasts hydrazine-dependent dinitrogen formation measured by mass spectrometry as the consequence of short saturating light flashes is always linked to a substantial oxygen uptake (G. Renger, K. P. Bader, and G. H. Schmid, Biochim. Biophys. Acta 1015, 288, 1990). However, in thylakoids of the filamentous cyanobacterium Oscillatoria chalybea this dinitrogen formation is not linked to an apparent O2-uptake, even at the high concentration of 1 mм hydrazine. Whereas in tobacco chloroplasts Tris-treatment does not affect hydrazine dependent dinitrogen formation up to a concentration of 3 mм hydrazine, Tris-treatment of thylakoids of O. chalybea affects strongly both oxygen evolution and dinitrogen evolution under a single turnover flash as well as under ten flashes. In contrast to tobacco chloroplasts, the presence of hydrazine up to concentrations of 3 mм does not substantially affect photosynthetic O2-evolution. The observed dinitrogen evolution is affected by DCMU regardless whether induced by a single turnover flash or by ten flashes, whereas in tobacco dinitrogen evolution and the O2-uptake linked to it (which is not observed in the cyanobacterium) were clearly not affected by DCMU in the single turnover flash. In Oscillatoria the earlier described Photosystem II-mediated H2O2 formation and decomposition is influenced by hydrazine. In the presence of 300 μм hydrazine the usually present O2-uptake leading to H2O2 formation appears diminished.

Interrelationship of Oxygen and Nitrogen Metabolism in the Filamentous Cyanobacterium Oscillatoria chalybea

1989 ◽  
Vol 44 (11-12) ◽  
pp. 946-954 ◽  
Author(s):  
J. Bednarz ◽  
S. Höper ◽  
M. Bockstette ◽  
K. P. Bader ◽  
G. H. Schmid
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Nitrate Reductase ◽  
Nitrogen Source ◽  
Nitrogen Metabolism ◽  
Light Illumination ◽  
Filamentous Cyanobacterium ◽  
Sole Nitrogen Source ◽  
Light Intensities ◽  
Oscillatoria Chalybea

Abstract Filamentous Cyanobacteria. Hydrogen Peroxide, Photosystem II. Nitrogen Metabolism By means of mass spectrometric analysis we have been able to demonstrate H 20 2-production and its decomposition by photosystem II in thylakoids of the filamentous cyanobacterium Oscil­ latoria chalybea. This H2O2-production and its quasi simultaneous decomposition by the S-state system can be readily demonstrated in flash light illumination (K. P. Bader and G. H. Schmid, Biochim. Biophys. Acta 936, 179-186 (1988)) or as shown in the present paper in continuous light at low light intensities. These light conditions correspond essentially to the culturing condition of the organism on nitrate as the sole nitrogen source. Under these conditions, however, electron transport between the two photosystems seems to be mostly disconnected and respiratory activity practically non existent. Under these conditions, on the other hand, nitrate reductase is induced and nitrate reduced. The present paper addresses the question how this organism might solve the metabolic problems of nitrate reduction with such an electron transport system. Tested under high light intensities under which the organism would not grow at all, electron transport between the two photosystems is optimally linked and the system funnels part of its photosynthetically pro­duced electrons into a conventional cyanide-sensitive respiratory electron transport chain and even into an alternative Sham-sensitive (cyanide-insensitive) respiratory chain. This is made possible by the overweight of photosystem II capacity in comparison to photosystem I activity as reported in this paper. Under the conditions described, the cyanobacterium grows also on ar­ginine as the sole nitrogen source. Most interestingly under these conditions nitrate reductase induction is not shut off as is the case with other aminoacids like ornithine or alanine in the medium. Nitrite reductase is not induced in these bacteria, if grown on arginine as the sole nitrogen source. This observation is discussed in context with the fact that arginine is a major storage product (cyanophycin) in this organism and that the observed photosystem II mediated H2O2-production might be correlated with arginine metabolism.

Independently Acting Oxygen-Forming Complexes of Photosystem II in Cyanobacteria A Study in the Filamentous Cyanobacterium Oscillatoria chalybea

1997 ◽  
Vol 52 (3-4) ◽  
pp. 169-174 ◽  
Author(s):  
S. Spiegel ◽  
K. Burda ◽  
K. P. Bader ◽  
G. H. Schmid
Keyword(s):  
Photosystem Ii ◽  
Cross Sections ◽  
Dark Adaptation ◽  
Filamentous Cyanobacterium ◽  
Damped Oscillations ◽  
Synechococcus Leopoliensis ◽  
Evolution Pattern ◽  
Oscillatoria Chalybea ◽  
The Individual ◽  
Oxygen Evolving

Abstract It has been postulated that the oxygen-evolving centers of photosystem II do not operate independently in the cyanobacterium Synechococcus leopoliensis in contrast to those of the chlorophyte Chlorella vulgaris and the diatom Phaeodactylum tricornutum (Mauzerall and Dubinsky (1993), Biochim. Biophys. Acta 1183, 123-129). Dependence would mean the existence of charge transfer among adjacent units and would be manifested by different saturation curves for the individual flashes of a sequence (different cross-sections), stronger damped oscillations and oxygen formation under the first flash, independently of the length of dark adaptation. We show in the present publication that in the filamentous cyanobacterium Oscillatoria chalybea the O2-evolution pattern which shows an O2-signal under the first flash (despite dark adaptation) can be explained within the heterogeneous Kok-model, assuming a non-standard initial S-state distribution (Bader, Thibault and Schmid (1983), Z. Naturforsch. 38c. 778-792).

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