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Schröder, Wolfgang P.ORCID iD iconorcid.org/0000-0001-9831-1533
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Publications (10 of 67) Show all publications
Hussein, R., Graça, A. T., Forsman, J., Aydin, A. O., Hall, M., Gaetcke, J., . . . Schröder, W. P. (2024). Cryo-electron microscopy reveals hydrogen positions and water networks in photosystem II. Science, 384(6702), 1349-1355
Open this publication in new window or tab >>Cryo-electron microscopy reveals hydrogen positions and water networks in photosystem II
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2024 (English)In: Science, ISSN 0036-8075, E-ISSN 1095-9203, Vol. 384, no 6702, p. 1349-1355Article in journal (Refereed) Published
Abstract [en]

Photosystem II starts the photosynthetic electron transport chain that converts solar energy into chemical energy and thus sustains life on Earth. It catalyzes two chemical reactions: water oxidation to molecular oxygen and plastoquinone reduction. Coupling of electron and proton transfer is crucial for efficiency; however, the molecular basis of these processes remains speculative owing to uncertain water binding sites and the lack of experimentally determined hydrogen positions. We thus collected high-resolution cryo-electron microscopy data of fully hydrated photosystem II from the thermophilic cyanobacterium Thermosynechococcus vestitus to a final resolution of 1.71 angstroms. The structure reveals several previously undetected partially occupied water binding sites and more than half of the hydrogen and proton positions. This clarifies the pathways of substrate water binding and plastoquinone B protonation.

Place, publisher, year, edition, pages
American Association for the Advancement of Science (AAAS), 2024
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-227578 (URN)10.1126/science.adn6541 (DOI)38900892 (PubMedID)2-s2.0-85196874000 (Scopus ID)
Funder
Swedish Research Council, 2020-03809Carl Tryggers foundation , 19.324The Kempe Foundations, JCK-2030 2021-2023
Available from: 2024-07-01 Created: 2024-07-01 Last updated: 2024-07-05Bibliographically approved
Shevela, D., Schröder, W. P. & Messinger, J. (2024). Measurements of oxygen evolution in photosynthesis (2ed.). In: Sarah Covshoff (Ed.), Photosynthesis: methods and protocols (pp. 133-148). New York: Humana Press, 2790
Open this publication in new window or tab >>Measurements of oxygen evolution in photosynthesis
2024 (English)In: Photosynthesis: methods and protocols / [ed] Sarah Covshoff, New York: Humana Press, 2024, 2, Vol. 2790, p. 133-148Chapter in book (Refereed)
Abstract [en]

This chapter compares two different techniques for monitoring photosynthetic O2 production; the wide-spread Clark-type O2 electrode and the more sophisticated membrane inlet mass spectrometry (MIMS) technique. We describe how a simple membrane inlet for MIMS can be made out of a commercial Clark-type cell and outline the advantages and drawbacks of the two techniques to guide researchers in deciding which method to use. Protocols and examples are given for measuring O2 evolution rates and for determining the number of chlorophyll molecules per active photosystem II reaction center.

Place, publisher, year, edition, pages
New York: Humana Press, 2024 Edition: 2
Series
Methods in Molecular (MIMB), ISSN 1064-3745, E-ISSN 1940-6029 ; 2790
Keywords
Clark-type electrode, Membrane-inlet mass spectrometry, O2 evolution, Oxygenic photosynthesis, Photosynthetic water oxidation, Photosynthetic water splitting, Photosystem II, Chlorophyll, Electrodes, Mass Spectrometry, Oxygen, Photosynthesis, Photosystem II Protein Complex, commercial phenomena, comparative study, controlled study, cost effectiveness analysis, desorption, electrochemical analysis, illumination, ion current, membrane, nonhuman, oxygen evolution, oxygen evolution reaction, pervaporation, water splitting, metabolism, procedures
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-224657 (URN)10.1007/978-1-0716-3790-6_8 (DOI)38649570 (PubMedID)2-s2.0-85191364750 (Scopus ID)978-1-0716-3789-0 (ISBN)978-1-0716-3792-0 (ISBN)978-1-0716-3790-6 (ISBN)
Funder
Swedish Research Council, 2020-03809Carl Tryggers foundation
Available from: 2024-05-22 Created: 2024-05-22 Last updated: 2024-07-05Bibliographically approved
Graça, A. T., Lihavainen, J., Hussein, R. & Schröder, W. P. (2024). Obscurity of chlorophyll tails - Is chlorophyll with farnesyl tail incorporated into PSII complexes?. Physiologia Plantarum, 176(4), Article ID e14428.
Open this publication in new window or tab >>Obscurity of chlorophyll tails - Is chlorophyll with farnesyl tail incorporated into PSII complexes?
2024 (English)In: Physiologia Plantarum, ISSN 0031-9317, E-ISSN 1399-3054, Vol. 176, no 4, article id e14428Article in journal (Refereed) Published
Abstract [en]

Chlorophyll is essential in photosynthesis, converting sunlight into chemical energy in plants, algae, and certain bacteria. Its structure, featuring a porphyrin ring enclosing a central magnesium ion, varies in forms like chlorophyll a, b, c, d, and f, allowing light absorption at a broader spectrum. With a 20-carbon phytyl tail (except for chlorophyll c), chlorophyll is anchored to proteins. Previous findings suggested the presence of chlorophyll with a modified farnesyl tail in thermophilic cyanobacteria Thermosynechoccocus vestitus. In our Arabidopsis thaliana PSII cryo-EM map, specific chlorophylls showed incomplete phytyl tails, suggesting potential farnesyl modifications. However, further high-resolution mass spectrometry (HRMS) analysis in A. thaliana and T. vestitus did not confirm the presence of any farnesyl tails. Instead, we propose the truncated tails in PSII models may result from binding pocket flexibility rather than actual modifications.

National Category
Botany
Identifiers
urn:nbn:se:umu:diva-227880 (URN)10.1111/ppl.14428 (DOI)2-s2.0-85197788105 (Scopus ID)
Funder
Carl Tryggers foundation , CTS19.324
Available from: 2024-07-15 Created: 2024-07-15 Last updated: 2024-07-15Bibliographically approved
Farci, D., Cocco, E., Tanas, M., Kirkpatrick, J., Maxia, A., Tamburini, E., . . . Piano, D. (2022). Isolation and characterization of a main porin from the outer membrane of Salinibacter ruber. Journal of Bioenergetics and Biomembranes, 54, 273-281
Open this publication in new window or tab >>Isolation and characterization of a main porin from the outer membrane of Salinibacter ruber
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2022 (English)In: Journal of Bioenergetics and Biomembranes, ISSN 0145-479X, E-ISSN 1573-6881, Vol. 54, p. 273-281Article in journal (Refereed) Published
Abstract [en]

Salinibacter ruber is an extremophilic bacterium able to grow in high-salts environments, such as saltern crystallizer ponds. This halophilic bacterium is red-pigmented due to the production of several carotenoids and their derivatives. Two of these pigment molecules, salinixanthin and retinal, are reported to be essential cofactors of the xanthorhodopsin, a light-driven proton pump unique to this bacterium. Here, we isolate and characterize an outer membrane porin-like protein that retains salinixanthin. The characterization by mass spectrometry identified an unknown protein whose structure, predicted by AlphaFold, consists of a 8 strands beta-barrel transmembrane organization typical of porins. The protein is found to be part of a functional network clearly involved in the outer membrane trafficking. Cryo-EM micrographs showed the shape and dimensions of a particle comparable with the ones of the predicted structure. Functional implications, with respect to the high representativity of this protein in the outer membrane fraction, are discussed considering its possible role in primary functions such as the nutrients uptake and the homeostatic balance. Finally, also a possible involvement in balancing the charge perturbation associated with the xanthorhodopsin and ATP synthase activities is considered.

Place, publisher, year, edition, pages
Springer, 2022
Keywords
Cryo-EM, Carotenoids, Halophile bacteria, Outer membrane, Outer membrane proteins, Cell envelope, Mass spectrometry, Salinibacter ruber
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-201378 (URN)10.1007/s10863-022-09950-7 (DOI)000867542600001 ()36229623 (PubMedID)2-s2.0-85139622006 (Scopus ID)
Available from: 2022-11-30 Created: 2022-11-30 Last updated: 2024-07-05Bibliographically approved
Cocco, E., Farci, D., Haniewicz, P., Schröder, W. P., Maxia, A. & Piano, D. (2022). The Influence of Blue and Red Light on Seed Development and Dormancy in Nicotiana tabacum L.. Seeds, 1(3), 152-163
Open this publication in new window or tab >>The Influence of Blue and Red Light on Seed Development and Dormancy in Nicotiana tabacum L.
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2022 (English)In: Seeds, ISSN 2674-1024, Vol. 1, no 3, p. 152-163Article in journal (Refereed) Published
Abstract [en]

The correct development of seeds is a pivotal requirement for species preservation. This process depends on the balance between sensing the environmental stimuli/stressors and hormone-mediated transduction, which results in physiological responses. The red and blue regions of the electromagnetic spectrum are known to influence seed dormancy and germination. Here, we report on the effects induced by the blue (peak at 430 nm) and red (peak at 650 nm) regions of the electromagnetic spectrum on seeds from photo- and skotomorphogenetic capsules developed under white, blue, or red light. Regardless of exposure, seeds from skotomorphogenetic capsules showed an almost absent dormancy in association with altered germination kinetics. Conversely, in seeds from photomorphogenetic capsules, the exposure to the blue region induced skotomorphogenetic-like effects, while the exposure to the whole visible range (350–750 nm), as well as to only the red region, showed a dose-related trend. The observed differences appeared to be dependent on the wavelengths in the red and to be based on transduction mechanisms taking place in fruits. While the molecular bases of this differential effect need to be clarified, the results hint at the role played by different light wavelengths and intensities in seed development and germination. These findings may be relevant for applications in crop production and species safeguarding.

Place, publisher, year, edition, pages
MDPI, 2022
Keywords
dormancy, germination, phytochrome, photomorphogenesis, skotomorphogenesis, Nicotiana tabacum cv. Petit Havana, etiolation, background fluorescence, maximum fluorescence, photosynthetic yield, chlorophyll protein content
National Category
Plant Biotechnology
Identifiers
urn:nbn:se:umu:diva-200051 (URN)10.3390/seeds1030014 (DOI)
Funder
Carl Tryggers foundation , CTS 19:324
Available from: 2022-10-06 Created: 2022-10-06 Last updated: 2024-07-05Bibliographically approved
Graça, A. T., Hall, M., Persson, K. & Schröder, W. P. (2021). High-resolution model of Arabidopsis Photosystem II reveals the structural consequences of digitonin-extraction. Scientific Reports, 11(1), Article ID 15534.
Open this publication in new window or tab >>High-resolution model of Arabidopsis Photosystem II reveals the structural consequences of digitonin-extraction
2021 (English)In: Scientific Reports, E-ISSN 2045-2322, Vol. 11, no 1, article id 15534Article in journal (Refereed) Published
Abstract [en]

In higher plants, the photosynthetic process is performed and regulated by Photosystem II (PSII). Arabidopsis thaliana was the first higher plant with a fully sequenced genome, conferring it the status of a model organism; nonetheless, a high-resolution structure of its Photosystem II is missing. We present the first Cryo-EM high-resolution structure of Arabidopsis PSII supercomplex with average resolution of 2.79 Å, an important model for future PSII studies. The digitonin extracted PSII complexes demonstrate the importance of: the LHG2630-lipid-headgroup in the trimerization of the light-harvesting complex II; the stabilization of the PsbJ subunit and the CP43-loop E by DGD520-lipid; the choice of detergent for the integrity of membrane protein complexes. Furthermore, our data shows at the anticipated Mn4CaO5-site a single metal ion density as a reminiscent early stage of Photosystem II photoactivation.

Place, publisher, year, edition, pages
Nature Publishing Group, 2021
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-186557 (URN)10.1038/s41598-021-94914-x (DOI)000683319500011 ()2-s2.0-85111686355 (Scopus ID)
Available from: 2021-08-11 Created: 2021-08-11 Last updated: 2024-07-05Bibliographically approved
Bag, P., Schröder, W. P., Jansson, S. & Farci, D. (2021). Solubilization method for isolation of photosynthetic mega- And super-complexes from conifer thylakoids. Bio-protocol, 11(17), Article ID e4144.
Open this publication in new window or tab >>Solubilization method for isolation of photosynthetic mega- And super-complexes from conifer thylakoids
2021 (English)In: Bio-protocol, E-ISSN 2331-8325, Vol. 11, no 17, article id e4144Article in journal (Refereed) Published
Abstract [en]

Photosynthesis is the main process by which sunlight is harvested and converted into chemical energy and has been a focal point of fundamental research in plant biology for decades. In higher plants, the process takes place in the thylakoid membranes where the two photosystems (PSI and PSII) are located. In the past few decades, the evolution of biophysical and biochemical techniques allowed detailed studies of the thylakoid organization and the interaction between protein complexes and cofactors. These studies have mainly focused on model plants, such as Arabidopsis, pea, spinach, and tobacco, which are grown in climate chambers even though significant differences between indoor and outdoor growth conditions are present. In this manuscript, we present a new mild-solubilization procedure for use with “fragile” samples such as thylakoids from conifers growing outdoors. Here, the solubilization protocol is optimized with two detergents in two species, namely Norway spruce (Picea abies) and Scots pine (Pinus sylvestris). We have optimized the isolation and characterization of PSI and PSII multimeric mega- and super-complexes in a close-to-native condition by Blue-Native gel electrophoresis. Eventually, our protocol will not only help in the characterization of photosynthetic complexes from conifers but also in understanding winter adaptation.

Keywords
2nd Dimension SDS-PAGE, Blue-Native gel electrophoresis, Norway spruce, Photosystem I, Photosystem II, Picea abies, Pinus sylvestris, Scots pine, Thylakoids
National Category
Botany Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-191367 (URN)10.21769/BioProtoc.4144 (DOI)000694707900012 ()34604449 (PubMedID)2-s2.0-85116025854 (Scopus ID)
Available from: 2022-01-14 Created: 2022-01-14 Last updated: 2024-07-05Bibliographically approved
Chen, Y.-E., Yuan, S., Lezhneva, L., Meurer, J., Schwenkert, S., Mamedov, F. & Schröder, W. P. (2019). The Low Molecular Mass Photosystem II Protein PsbTn is Important for Light Acclimation. Plant Physiology, 179(4), 1739-1753
Open this publication in new window or tab >>The Low Molecular Mass Photosystem II Protein PsbTn is Important for Light Acclimation
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2019 (English)In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 179, no 4, p. 1739-1753Article in journal (Refereed) Published
Abstract [en]

Photosystem II (PSII) is a supramolecular complex containing over 30 protein subunits and a large set of cofactors including various pigments and quinones as well as Mn, Ca, Cl, and Fe ions. Eukaryotic PSII complexes contain many subunits not found in their bacterial counterparts, including the proteins PsbP, PsbQ, PsbS, and PsbW, as well as the highly homologous, low molecular mass subunits PsbTn1 and PsbTn2 whose function is currently unknown. To determine the function of PsbTn1 and PsbTn2, we generated single and double psbTn1 and psbTn2 knock-out mutants in Arabidopsis thaliana. Cross-linking and reciprocal co-immunoprecipitation experiments revealed that PsbTn is a lumenal PSII protein situated next to the cytochrome b559 subunit PsbE. The removal of the PsbTn proteins decreased the oxygen evolution rate and PSII core phosphorylation level but increased the susceptibility of PSII to photoinhibition and the production of reactive oxygen species. The assembly and stability of PSII were unaffected, indicating that the deficiencies of the psbTn1 psbTn2 double mutants are due to structural changes. Double mutants exhibited a higher rate of non-photochemical quenching of excited states than the wild type and single mutants, as well as slower state transition kinetics and a lower quantum yield of PSII when grown in the field. Based on these results, we propose that the main function of the PsbTn proteins is to enable PSII to acclimate to light shifts or intense illumination.

Place, publisher, year, edition, pages
Rockville: American Society of Plant Biologists, 2019
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-156389 (URN)10.1104/pp.18.01251 (DOI)000462993100045 ()30538167 (PubMedID)2-s2.0-85064206650 (Scopus ID)
Funder
Carl Tryggers foundation
Note

Short title: PsbTn protein regulates light adaptation

Available from: 2019-02-14 Created: 2019-02-14 Last updated: 2024-07-05Bibliographically approved
Dubreuil, C., Jin, X., Barajas-López, J. d., Hewitt, T. C., Tanz, S. K., Dobrenel, T., . . . Strand, Å. (2018). Establishment of Photosynthesis through Chloroplast Development Is Controlled by Two Distinct Regulatory Phases. Plant Physiology, 176(2), 1199-1214
Open this publication in new window or tab >>Establishment of Photosynthesis through Chloroplast Development Is Controlled by Two Distinct Regulatory Phases
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2018 (English)In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 176, no 2, p. 1199-1214Article in journal (Refereed) Published
Abstract [en]

Chloroplasts develop from undifferentiated proplastids present in meristematic tissue. Thus, chloroplast biogenesis is closely connected to leaf development, which restricts our ability to study the process of chloroplast biogenesis per se. As a consequence, we know relatively little about the regulatory mechanisms behind the establishment of the photosynthetic reactions and how the activities of the two genomes involved are coordinated during chloroplast development. We developed a single cell-based experimental system from Arabidopsis (Arabidopsis thaliana) with high temporal resolution allowing for investigations of the transition from proplastids to functional chloroplasts. Using this unique cell line, we could show that the establishment of photosynthesis is dependent on a regulatory mechanism involving two distinct phases. The first phase is triggered by rapid light-induced changes in gene expression and the metabolome. The second phase is dependent on the activation of the chloroplast and generates massive changes in the nuclear gene expression required for the transition to photosynthetically functional chloroplasts. The second phase also is associated with a spatial transition of the chloroplasts from clusters around the nucleus to the final position at the cell cortex. Thus, the establishment of photosynthesis is a two-phase process with a clear checkpoint associated with the second regulatory phase allowing coordination of the activities of the nuclear and plastid genomes.

Place, publisher, year, edition, pages
American Society of Plant Biologists, 2018
National Category
Botany
Identifiers
urn:nbn:se:umu:diva-140157 (URN)10.1104/pp.17.00435 (DOI)000424285500021 ()28626007 (PubMedID)2-s2.0-85041733632 (Scopus ID)
Projects
Bio4Energy
Funder
Bio4Energy
Available from: 2017-10-02 Created: 2017-10-02 Last updated: 2024-07-02Bibliographically approved
Shevela, D., Schröder, W. P. & Messinger, J. (2018). Liquid-phase measurements of photosynthetic oxygen evolution. Methods in Molecular Biology, 1770, 197-211
Open this publication in new window or tab >>Liquid-phase measurements of photosynthetic oxygen evolution
2018 (English)In: Methods in Molecular Biology, ISSN 1064-3745, E-ISSN 1940-6029, Vol. 1770, p. 197-211Article in journal (Refereed) Published
Abstract [en]

This chapter compares two different techniques for monitoring photosynthetic O2 production: the widespread Clark-type O2 electrode and the more sophisticated membrane inlet mass spectrometry (MIMS) technique. We describe how a simple membrane inlet for MIMS can be made out of a commercial Clark-type cell, and outline the advantages and drawbacks of the two techniques to guide researchers in deciding which method to use. Protocols and examples are given for measuring O2 evolution rates and for determining the number of chlorophyll molecules per active photosystem II reaction center.

Keywords
Photosynthetic water oxidation, O2 evolution, Photosystem II, Clark-type electrode, Membrane inlet mass spectrometry
National Category
Biophysics
Identifiers
urn:nbn:se:umu:diva-152593 (URN)10.1007/978-1-4939-7786-4_11 (DOI)29978403 (PubMedID)2-s2.0-85049684999 (Scopus ID)
Available from: 2018-10-15 Created: 2018-10-15 Last updated: 2024-07-02Bibliographically approved
Projects
Regulatory roles of small, nuclear-encoded proteins in the organisation of macro-complexes in photosynthetic membranes [2008-03207_VR]; Umeå University
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0001-9831-1533

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