Effect of MgCl2 and Phosphatidylglycerol on CaCl2-Mediated Recovery of Oxygen Evolution in a Photosystem II Complex Depleted of the 17 and 24 kDa Extrinsic Proteins

1998 ◽  
Vol 53 (1-2) ◽  
pp. 39-48 ◽  
Author(s):  
E. K. Nénonéné ◽  
M. Méthot ◽  
M. Fragata
Keyword(s):  
Oxygen Evolution ◽  
Water Oxidation ◽  
Higher Plants ◽  
Molecular System ◽  
Chloride Ions ◽  
Core Complex ◽  
Higher Plant ◽  
Oscillatoria Chalybea ◽  
Extrinsic Proteins ◽  
Psii Core Complex

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],

scholarly journals Electronic Structure of Tyrosyl D Radical of Photosystem II, as Revealed by 2D-Hyperfine Sublevel Correlation Spectroscopy

2021 ◽  
Vol 7 (9) ◽  
pp. 131
Author(s):  
Maria Chrysina ◽  
Georgia Zahariou ◽  
Nikolaos Ioannidis ◽  
Yiannis Sanakis ◽  
George Mitrikas
Keyword(s):  
Electronic Structure ◽  
Photosystem Ii ◽  
Water Oxidation ◽  
Spinacia Oleracea ◽  
Higher Plants ◽  
Correlation Spectroscopy ◽  
Oxygen Evolving Complex ◽  
Higher Plant ◽  
Proton Coupled Electron Transfer ◽  
S Oxidation

The biological water oxidation takes place in Photosystem II (PSII), a multi-subunit protein located in thylakoid membranes of higher plant chloroplasts and cyanobacteria. The catalytic site of PSII is a Mn4Ca cluster and is known as the oxygen evolving complex (OEC) of PSII. Two tyrosine residues D1-Tyr161 (YZ) and D2-Tyr160 (YD) are symmetrically placed in the two core subunits D1 and D2 and participate in proton coupled electron transfer reactions. YZ of PSII is near the OEC and mediates electron coupled proton transfer from Mn4Ca to the photooxidizable chlorophyll species P680+. YD does not directly interact with OEC, but is crucial for modulating the various S oxidation states of the OEC. In PSII from higher plants the environment of YD• radical has been extensively characterized only in spinach (Spinacia oleracea) Mn- depleted non functional PSII membranes. Here, we present a 2D-HYSCORE investigation in functional PSII of spinach to determine the electronic structure of YD• radical. The hyperfine couplings of the protons that interact with the YD• radical are determined and the relevant assignment is provided. A discussion on the similarities and differences between the present results and the results from studies performed in non functional PSII membranes from higher plants and PSII preparations from other organisms is given.

scholarly journals Evidence for two-step processing of nuclear-encoded chloroplast proteins during membrane assembly.

1986 ◽  
Vol 103 (3) ◽  
pp. 725-731 ◽  
Author(s):  
C P Chia ◽  
C J Arntzen
Keyword(s):  
Water Oxidation ◽  
Size Class ◽  
Proteolytic Processing ◽  
Chloroplast Envelope ◽  
Second Step ◽  
Core Complex ◽  
Intermediate Size ◽  
Polymorphic Forms ◽  
Inside Out ◽  
Psii Core Complex

A plastome (chloroplast genome) mutant of tobacco, lutescens-1, displays abnormal degradation of the chloroplast-encoded polypeptides which form the core complex of photosystem II (PSII). Two nuclear-encoded proteins (present in polymorphic forms), which normally function in the water oxidation process of PSII, accumulate as larger size-class polypeptides in mutant thylakoid membranes. These accumulated proteins are intermediate in size between the full-length primary protein synthesized in the cytoplasm and the proteolytically processed mature polypeptides. Trypsin treatment of unstacked mutant thylakoids and of inside-out vesicle (PSII-enriched) preparations indicated that the intermediate size forms were correctly localized on the inner surface of the thylakoid membrane, but not surface-exposed in the same way as the mature proteins. Only one of the intermediate size-class proteins could be extracted by salt washes. We interpret these data to be consistent with the idea that the two imported proteins that function in the water oxidation step of photosynthesis and are localized in the loculus (the space within the thylakoid vesicles) undergo two-step processing. The second step in proteolytic processing may be related to transport through a second membrane (the first transport step through the chloroplast envelope having been completed); this step may be arrested in the mutant due to the absence of the PSII core complex.

scholarly journals Mass Spectrometry-based Footprinting Reveals Structural Dynamics of Loop E of the Chlorophyll-binding Protein CP43 during Photosystem II Assembly in the Cyanobacterium Synechocystis 6803

2013 ◽  
Vol 288 (20) ◽  
pp. 14212-14220 ◽  
Author(s):  
Haijun Liu ◽  
Jiawei Chen ◽  
Richard Y.-C. Huang ◽  
Daniel Weisz ◽  
Michael L. Gross ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Water Oxidation ◽  
Higher Plants ◽  
Protein A ◽  
D1 Protein ◽  
Cluster Assembly ◽  
Conformational Rearrangement ◽  
Photosynthetic Organisms ◽  
Binding Interface ◽  
Extrinsic Proteins

The PSII repair cycle is required for sustainable photosynthesis in oxygenic photosynthetic organisms. In cyanobacteria and higher plants, proteolysis of the precursor D1 protein (pD1) to expose a C-terminal carboxylate group is an essential step leading to coordination of the Mn4CaO5 cluster, the site of water oxidation. Psb27 appears to associate with both pD1- and D1-containing PSII assembly intermediates by closely interacting with CP43. Here, we report that reduced binding affinity between CP43 and Psb27 is triggered by the removal of the C-terminal extension of the pD1 protein. A mass spectrometry-based footprinting strategy was adopted to probe solvent-exposed aspartic and glutamic acid residues on the CP43 protein. By comparing the extent of footprinting between HT3ΔctpAΔ27PSII and HT3ΔctpAPSII, two genetically modified PSII assembly complexes, we found that Psb27 binds to CP43 on the side of Loop E distal to the pseudo-symmetrical D1-D2 axis. By comparing a second pair of PSII assembly complexes, we discovered that Loop E of CP43 undergoes a significant conformational rearrangement due to the removal of the pD1 C-terminal extension, altering the Psb27-CP43 binding interface. The significance of this conformational rearrangement is discussed in the context of recruitment of the PSII lumenal extrinsic proteins and Mn4CaO5 cluster assembly. In addition to CP43's previously known function as one of the core PSII antenna proteins, this work demonstrates that Loop E of CP43 plays an important role in the functional assembly of the Water Oxidizing Center (WOC) during PSII biogenesis.

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
Keyword(s):  
Oxygen Evolution ◽  
Green Alga ◽  
Signal Amplitude ◽  
Blue Green Alga ◽  
State Distribution ◽  
Higher Plant ◽  
Experimental Conditions ◽  
Oscillatoria Chalybea ◽  
Electrochemical Signal ◽  
High Level

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.

Controllable growth of graphdiyne layered nanosheets for high-performance water oxidation

2021 ◽  
Author(s):  
Shuya Zhao ◽  
Yurui Xue ◽  
Zhongqiang Wang ◽  
Zhiqiang Zheng ◽  
Xiaoyu Luan ◽  
...  
Keyword(s):  
Oxygen Evolution ◽  
Oxygen Evolution Reaction ◽  
Water Oxidation ◽  
High Performance ◽  
Low Cost ◽  
Highly Active ◽  
Controllable Growth

Developing highly active, stable and low-cost electrocatalysts capable of an efficient oxygen evolution reaction (OER) is urgent and challenging.

Bifunctional citrate-Ni0.9Co0.1(OH)x layer coated fluorine-doped hematite for simultaneous hole extraction and injection towards efficient photoelectrochemical water oxidation

Nanoscale ◽  
2021 ◽  
Author(s):  
Peng Wang ◽  
Feng Li ◽  
Xuefeng Long ◽  
Tong Wang ◽  
Huan Chai ◽  
...  
Keyword(s):  
Surface Modification ◽  
Oxygen Evolution ◽  
Oxygen Evolution Reaction ◽  
Water Oxidation ◽  
Surface Oxygen ◽  
Co Catalyst ◽  
Photoelectrochemical Water Oxidation

Surface modification by loading a water oxidation co-catalyst (WOC) is generally considered to be an efficient means to optimize the sluggish surface oxygen evolution reaction (OER) of hematite photoanode for...

Rutile TiO2 single crystals delivering enhanced photocatalytic oxygen evolution performance

Nanoscale ◽  
2021 ◽  
Author(s):  
Bing Fu ◽  
Zhijiao Wu ◽  
Kai Guo ◽  
Lingyu Piao
Keyword(s):  
Catalytic Activity ◽  
Single Crystals ◽  
Oxygen Evolution ◽  
Water Oxidation ◽  
Charge Separation ◽  
High Surface ◽  
Rutile Tio2 ◽  
Highly Efficient ◽  
Photogenerated Charge Separation

Owing to their scientific and technological importance, the development of highly efficient photocatalytic water oxidation systems with rapid photogenerated charge separation and high surface catalytic activity has highly desirable for...

Oriental and robust anchoring of Fe via anodic interfacial coordination assembly on ultrathin Co hydroxides for efficient water oxidation

Nanoscale ◽  
2021 ◽  
Author(s):  
Ya-Nan Zhou ◽  
Ruo-Yao Fan ◽  
Yu-Ning Cao ◽  
Hui-Ying Wang ◽  
Bin Dong ◽  
...  
Keyword(s):  
Oxygen Evolution ◽  
Oxygen Evolution Reaction ◽  
Water Oxidation ◽  
Active Sites

The oriental distribution and strong conjunction of Fe active sites in multiple metals hydroxides are very crucial to modulate the activity and stability for efficient oxygen evolution reaction (OER). Whereas,...

scholarly journals Effect of alkaline pH on photosynthetic water oxidation and the association of extrinsic proteins with Photosystem Two

1989 ◽  
Vol 258 (2) ◽  
pp. 357-362 ◽  
Author(s):  
D J Chapman ◽  
J De Felice ◽  
K Davis ◽  
J Barber
Keyword(s):  
Water Splitting ◽  
Water Oxidation ◽  
Binding Sites ◽  
Partial Recovery ◽  
Alkaline Ph ◽  
Ph Values ◽  
Extrinsic Proteins ◽  
Reversible Phase ◽  
Photosynthetic Water Oxidation ◽  
Optimal Ph

Incubation of a membrane preparation enriched in Photosystem Two (PSII) at alkaline pH inhibited the water-splitting reactions in two distinct steps. Up to pH 8.5 the inhibition was reversible, whereas at higher alkalinities it was irreversible. It was shown that the reversible phase correlated with loss and rebinding of the 23 kDa extrinsic polypeptide. However, after mild alkaline treatments a partial recovery was possible without the binding of the 23 kDa polypeptide when the assay was at the optimal pH of 6.5 and in a medium containing excess Cl-. The irreversible phase was found to be closely linked with the removal of the 33 kDa extrinsic protein of PSII. Treatments with pH values above 8.5 not only caused the 33 kDa protein to be displaced from the PSII-enriched membranes, but also resulted in an irreversible modification of the binding sites such that the extrinsic 33 kDa protein could not reassociate with PSII when the pH was lowered to 6.5. The results obtained with these more extreme alkaline pH treatments support the notion that the 23 kDa protein cannot bind to PSII unless the 33 kDa protein is already bound. The differential effect of pH on the removal of the 23 kDa and 33 kDa proteins contrasted with the data of Kuwabara & Murata [(1983) Plant Cell Physiol. 24, 741-747], but this discrepancy was accounted for by the use of glycerol in the incubation media.

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