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Publications (10 of 128) Show all publications
de Lichtenberg, C., Rapatskiy, L., Reus, M., Heyno, E., Schnegg, A., Nowaczyk, M. M., . . . Cox, N. (2024). Assignment of the slowly exchanging substrate water of nature's water-splitting cofactor. Proceedings of the National Academy of Sciences of the United States of America, 121(11), Article ID e2319374121.
Open this publication in new window or tab >>Assignment of the slowly exchanging substrate water of nature's water-splitting cofactor
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2024 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 121, no 11, article id e2319374121Article in journal (Refereed) Published
Abstract [en]

Identifying the two substrate water sites of nature's water-splitting cofactor (Mn4CaO5 cluster) provides important information toward resolving the mechanism of O-O bond formation in Photosystem II (PSII). To this end, we have performed parallel substrate water exchange experiments in the S1 state of native Ca-PSII and biosynthetically substituted Sr-PSII employing Time-Resolved Membrane Inlet Mass Spectrometry (TR-MIMS) and a Time-Resolved 17O-Electron-electron Double resonance detected NMR (TR-17O-EDNMR) approach. TR-MIMS resolves the kinetics for incorporation of the oxygen-isotope label into the substrate sites after addition of H218O to the medium, while the magnetic resonance technique allows, in principle, the characterization of all exchangeable oxygen ligands of the Mn4CaO5 cofactor after mixing with H217O. This unique combination shows i) that the central oxygen bridge (O5) of Ca-PSII core complexes isolated from Thermosynechococcus vestitus has, within experimental conditions, the same rate of exchange as the slowly exchanging substrate water (WS) in the TR-MIMS experiments and ii) that the exchange rates of O5 and WS are both enhanced by Ca2+→Sr2+ substitution in a similar manner. In the context of previous TR-MIMS results, this shows that only O5 fulfills all criteria for being WS. This strongly restricts options for the mechanism of water oxidation.

Place, publisher, year, edition, pages
Proceedings of the National Academy of Sciences (PNAS), 2024
Keywords
electron paramagnetic resonance (EPR), membrane inlet mass spectrometry (MIMS), photosynthesis, photosystem II, water oxidation mechanism
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-222362 (URN)10.1073/pnas.2319374121 (DOI)38437550 (PubMedID)2-s2.0-85186844144 (Scopus ID)
Funder
Max Planck SocietySwedish Research Council, 2016-05183Swedish Research Council, 2020-03809
Available from: 2024-03-15 Created: 2024-03-15 Last updated: 2024-03-15Bibliographically approved
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
Guo, Y., Messinger, J., Kloo, L. & Sun, L. (2023). Alternative mechanism for O2formation in natural photosynthesis via nucleophilic Oxo-Oxo coupling. Journal of the American Chemical Society, 145(7), 4129-4141
Open this publication in new window or tab >>Alternative mechanism for O2formation in natural photosynthesis via nucleophilic Oxo-Oxo coupling
2023 (English)In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 145, no 7, p. 4129-4141Article in journal (Refereed) Published
Abstract [en]

O2 formation in photosystem II (PSII) is a vital event on Earth, but the exact mechanism remains unclear. The presently prevailing theoretical model is "radical coupling"(RC) involving a Mn(IV)-oxyl unit in an "open-cubane"Mn4CaO6 cluster, which is supported experimentally by the S3 state of cyanobacterial PSII featuring an additional Mn-bound oxygenic ligand. However, it was recently proposed that the major structural form of the S3 state of higher plants lacks this extra ligand, and that the resulting S4 state would feature instead a penta-coordinate dangler Mn(V)=oxo, covalently linked to a "closed-cubane"Mn3CaO4 cluster. For this proposal, we explore here a large number of possible pathways of O-O bond formation and demonstrate that the "nucleophilic oxo-oxo coupling"(NOOC) between Mn(V)=oxo and μ3-oxo is the only eligible mechanism in such a system. The reaction is facilitated by a specific conformation of the cluster and concomitant water binding, which is delayed compared to the RC mechanism. An energetically feasible process is described starting from the valid S4 state through the sequential formation of peroxide and superoxide, followed by O2 release and a second water insertion. The newly found mechanism is consistent with available experimental thermodynamic and kinetic data and thus a viable alternative pathway for O2 formation in natural photosynthesis, in particular for higher plants.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2023
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-205197 (URN)10.1021/jacs.2c12174 (DOI)000936768400001 ()36763485 (PubMedID)2-s2.0-85147993483 (Scopus ID)
Funder
Swedish Research Council, 2020-03809Swedish Energy Agency, 45421-1
Available from: 2023-02-28 Created: 2023-02-28 Last updated: 2023-09-05
Simon, P. S., Makita, H., Bogacz, I., Fuller, F., Bhowmick, A., Hussein, R., . . . Yano, J. (2023). Capturing the sequence of events during the water oxidation reaction in photosynthesis using XFELs. FEBS Letters, 597(1), 30-37
Open this publication in new window or tab >>Capturing the sequence of events during the water oxidation reaction in photosynthesis using XFELs
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2023 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 597, no 1, p. 30-37Article, review/survey (Refereed) Published
Abstract [en]

Ever since the discovery that Mn was required for oxygen evolution in plants by Pirson in 1937 and the period-four oscillation in flash-induced oxygen evolution by Joliot and Kok in the 1970s, understanding of this process has advanced enormously using state-of-the-art methods. The most recent in this series of innovative techniques was the introduction of X-ray free-electron lasers (XFELs) a decade ago, which led to another quantum leap in the understanding in this field, by enabling operando X-ray structural and X-ray spectroscopy studies at room temperature. This review summarizes the current understanding of the structure of Photosystem II (PS II) and its catalytic centre, the Mn4CaO5 complex, in the intermediate Si (i = 0–4)-states of the Kok cycle, obtained using XFELs.

Place, publisher, year, edition, pages
John Wiley & Sons, 2023
Keywords
manganese metalloenzymes, oxygen evolving complex, photosystem II, water-oxidation/splitting, X-ray free-electron laser, X-ray spectroscopy
National Category
Physical Chemistry Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-201329 (URN)10.1002/1873-3468.14527 (DOI)000883333900001 ()36310373 (PubMedID)2-s2.0-85142148043 (Scopus ID)
Note

Special Issue: Visions of bio-inorganic chemistry: Metals and the molecules of life

Available from: 2022-12-15 Created: 2022-12-15 Last updated: 2023-03-24Bibliographically approved
Hussein, R., Ibrahim, M., Bhowmick, A., Simon, P. S., Bogacz, I., Doyle, M. D., . . . Yano, J. (2023). Evolutionary diversity of proton and water channels on the oxidizing side of photosystem II and their relevance to function. Photosynthesis Research, 158(2), 91-107
Open this publication in new window or tab >>Evolutionary diversity of proton and water channels on the oxidizing side of photosystem II and their relevance to function
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2023 (English)In: Photosynthesis Research, ISSN 0166-8595, E-ISSN 1573-5079, Vol. 158, no 2, p. 91-107Article, review/survey (Refereed) Published
Abstract [en]

One of the reasons for the high efficiency and selectivity of biological catalysts arise from their ability to control the pathways of substrates and products using protein channels, and by modulating the transport in the channels using the interaction with the protein residues and the water/hydrogen-bonding network. This process is clearly demonstrated in Photosystem II (PS II), where its light-driven water oxidation reaction catalyzed by the Mn4CaO5 cluster occurs deep inside the protein complex and thus requires the transport of two water molecules to and four protons from the metal center to the bulk water. Based on the recent advances in structural studies of PS II from X-ray crystallography and cryo-electron microscopy, in this review we compare the channels that have been proposed to facilitate this mass transport in cyanobacteria, red and green algae, diatoms, and higher plants. The three major channels (O1, O4, and Cl1 channels) are present in all species investigated; however, some differences exist in the reported structures that arise from the different composition and arrangement of membrane extrinsic subunits between the species. Among the three channels, the Cl1 channel, including the proton gate, is the most conserved among all photosynthetic species. We also found at least one branch for the O1 channel in all organisms, extending all the way from Ca/O1 via the ‘water wheel’ to the lumen. However, the extending path after the water wheel varies between most species. The O4 channel is, like the Cl1 channel, highly conserved among all species while having different orientations at the end of the path near the bulk. The comparison suggests that the previously proposed functionality of the channels in T. vestitus (Ibrahim et al., Proc Natl Acad Sci USA 117:12624–12635, 2020; Hussein et al., Nat Commun 12:6531, 2021) is conserved through the species, i.e. the O1-like channel is used for substrate water intake, and the tighter Cl1 and O4 channels for proton release. The comparison does not eliminate the potential role of O4 channel as a water intake channel. However, the highly ordered hydrogen-bonded water wire connected to the Mn4CaO5 cluster via the O4 may strongly suggest that it functions in proton release, especially during the S0 → S1 transition (Saito et al., Nat Commun 6:8488, 2015; Kern et al., Nature 563:421–425, 2018; Ibrahim et al., Proc Natl Acad Sci USA 117:12624–12635, 2020; Sakashita et al., Phys Chem Chem Phys 22:15831–15841, 2020; Hussein et al., Nat Commun 12:6531, 2021).

Place, publisher, year, edition, pages
Springer Nature, 2023
Keywords
Evolution, Oxygen evolving complex, Photosystem II, Water oxidation, Water transport
National Category
Biophysics Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-209571 (URN)10.1007/s11120-023-01018-w (DOI)000999800000001 ()37266800 (PubMedID)2-s2.0-85160823588 (Scopus ID)
Funder
Swedish Energy Agency, 45421-1NIH (National Institutes of Health), EXC 2008/1-390540038, GM055302, GM110501, GM126289Swedish Research Council, 2020-03809
Available from: 2023-06-12 Created: 2023-06-12 Last updated: 2023-12-21Bibliographically approved
Bag, P., Shutova, T., Shevela, D., Lihavainen, J., Nanda, S., Ivanov, A. G., . . . Jansson, S. (2023). Flavodiiron-mediated O2 photoreduction at photosystem I acceptor-side provides photoprotection to conifer thylakoids in early spring. Nature Communications, 14(1), Article ID 3210.
Open this publication in new window or tab >>Flavodiiron-mediated O2 photoreduction at photosystem I acceptor-side provides photoprotection to conifer thylakoids in early spring
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2023 (English)In: Nature Communications, E-ISSN 2041-1723, Vol. 14, no 1, article id 3210Article in journal (Refereed) Published
Abstract [en]

Green organisms evolve oxygen (O2) via photosynthesis and consume it by respiration. Generally, net O2 consumption only becomes dominant when photosynthesis is suppressed at night. Here, we show that green thylakoid membranes of Scots pine (Pinus sylvestris L) and Norway spruce (Picea abies) needles display strong O2 consumption even in the presence of light when extremely low temperatures coincide with high solar irradiation during early spring (ES). By employing different electron transport chain inhibitors, we show that this unusual light-induced O2 consumption occurs around photosystem (PS) I and correlates with higher abundance of flavodiiron (Flv) A protein in ES thylakoids. With P700 absorption changes, we demonstrate that electron scavenging from the acceptor-side of PSI via O2 photoreduction is a major alternative pathway in ES. This photoprotection mechanism in vascular plants indicates that conifers have developed an adaptative evolution trajectory for growing in harsh environments.

Place, publisher, year, edition, pages
Springer Nature, 2023
National Category
Biochemistry and Molecular Biology Botany
Identifiers
urn:nbn:se:umu:diva-209538 (URN)10.1038/s41467-023-38938-z (DOI)001002562700001 ()37270605 (PubMedID)2-s2.0-85160880215 (Scopus ID)
Funder
EU, Horizon 2020, 675006Swedish Research Council, (2016-04894 aSwedish Research Council, 2021-05062Swedish Research Council, 2020-03809The Kempe Foundations, 2014Swedish Research Council Formas, 2015-00907Swedish Research Council Formas, 2021-01474Swedish Foundation for Strategic Research, FFF20- 0008Vinnova, 2016-00504Knut and Alice Wallenberg Foundation, 2016-0352Knut and Alice Wallenberg Foundation, 2020.0240Göran Gustafsson Foundation for Research in Natural Sciences and Medicine, BS2022-0021
Available from: 2023-06-13 Created: 2023-06-13 Last updated: 2024-07-02Bibliographically approved
Bhowmick, A., Simon, P. S., Bogacz, I., Hussein, R., Zhang, M., Makita, H., . . . Yano, J. (2023). Going around the Kok cycle of the water oxidation reaction with femtosecond X-ray crystallography. Paper presented at The IUCr 2023 Congress, 22-29 August 2023, Melbourne, Australia,. IUCrJ, 10(6), 642-655
Open this publication in new window or tab >>Going around the Kok cycle of the water oxidation reaction with femtosecond X-ray crystallography
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2023 (English)In: IUCrJ, E-ISSN 2052-2525, Vol. 10, no 6, p. 642-655Article, review/survey (Refereed) Published
Abstract [en]

The water oxidation reaction in photosystem II (PS II) produces most of the molecular oxygen in the atmosphere, which sustains life on Earth, and in this process releases four electrons and four protons that drive the downstream process of CO2 fixation in the photosynthetic apparatus. The catalytic center of PS II is an oxygen-bridged Mn4Ca complex (Mn4CaO5) which is progressively oxidized upon the absorption of light by the chlorophyll of the PS II reaction center, and the accumulation of four oxidative equivalents in the catalytic center results in the oxidation of two waters to dioxygen in the last step. The recent emergence of X-ray free-electron lasers (XFELs) with intense femtosecond X-ray pulses has opened up opportunities to visualize this reaction in PS II as it proceeds through the catalytic cycle. In this review, we summarize our recent studies of the catalytic reaction in PS II by following the structural changes along the reaction pathway via room-temperature X-ray crystallography using XFELs. The evolution of the electron density changes at the Mn complex reveals notable structural changes, including the insertion of OX from a new water molecule, which disappears on completion of the reaction, implicating it in the O-O bond formation reaction. We were also able to follow the structural dynamics of the protein coordinating with the catalytic complex and of channels within the protein that are important for substrate and product transport, revealing well orchestrated conformational changes in response to the electronic changes at the Mn4Ca cluster.

Place, publisher, year, edition, pages
International Union Of Crystallography, 2023
Keywords
manganese metalloenzymes, oxygen evolving complex, photosystem II, water-splitting, wateroxidation, X-ray free-electron lasers, X-ray spectroscopy
National Category
Structural Biology Organic Chemistry
Identifiers
urn:nbn:se:umu:diva-217019 (URN)10.1107/S2052252523008928 (DOI)2-s2.0-85176617926 (Scopus ID)
Conference
The IUCr 2023 Congress, 22-29 August 2023, Melbourne, Australia,
Available from: 2023-11-24 Created: 2023-11-24 Last updated: 2023-11-24Bibliographically approved
Shevela, D., Kern, J. F., Govindjee, G. & Messinger, J. (2023). Solar energy conversion by photosystem II: principles and structures. Photosynthesis Research, 156, 279-307
Open this publication in new window or tab >>Solar energy conversion by photosystem II: principles and structures
2023 (English)In: Photosynthesis Research, ISSN 0166-8595, E-ISSN 1573-5079, Vol. 156, p. 279-307Article, review/survey (Refereed) Published
Abstract [en]

Photosynthetic water oxidation by Photosystem II (PSII) is a fascinating process because it sustains life on Earth and serves as a blue print for scalable synthetic catalysts required for renewable energy applications. The biophysical, computational, and structural description of this process, which started more than 50 years ago, has made tremendous progress over the past two decades, with its high-resolution crystal structures being available not only of the dark-stable state of PSII, but of all the semi-stable reaction intermediates and even some transient states. Here, we summarize the current knowledge on PSII with emphasis on the basic principles that govern the conversion of light energy to chemical energy in PSII, as well as on the illustration of the molecular structures that enable these reactions. The important remaining questions regarding the mechanism of biological water oxidation are highlighted, and one possible pathway for this fundamental reaction is described at a molecular level.

Place, publisher, year, edition, pages
Springer, 2023
Keywords
Educational review, Function of Photosystem II, Mechanism of water oxidation, Oxygen evolution, Photosynthesis, Primary photochemistry
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-205354 (URN)10.1007/s11120-022-00991-y (DOI)000939349400001 ()36826741 (PubMedID)2-s2.0-85148637702 (Scopus ID)
Funder
Umeå UniversitySwedish Research Council, 2020-03809Swedish Energy Agency, 45421-1
Available from: 2023-03-30 Created: 2023-03-30 Last updated: 2023-07-14Bibliographically approved
Bhowmick, A., Hussein, R., Bogacz, I., Simon, P. S., Ibrahim, M., Chatterjee, R., . . . Yachandra, V. K. (2023). Structural evidence for intermediates during O2 formation in photosystem II. Nature, 617(7961), 629-636
Open this publication in new window or tab >>Structural evidence for intermediates during O2 formation in photosystem II
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2023 (English)In: Nature, ISSN 0028-0836, E-ISSN 1476-4687, Vol. 617, no 7961, p. 629-636Article in journal (Refereed) Published
Abstract [en]

In natural photosynthesis, the light-driven splitting of water into electrons, protons and molecular oxygen forms the first step of the solar-to-chemical energy conversion process. The reaction takes place in photosystem II, where the Mn4CaO5 cluster first stores four oxidizing equivalents, the S0 to S4 intermediate states in the Kok cycle, sequentially generated by photochemical charge separations in the reaction center and then catalyzes the O–O bond formation chemistry. Here, we report room temperature snapshots by serial femtosecond X-ray crystallography to provide structural insights into the final reaction step of Kok’s photosynthetic water oxidation cycle, the S3→[S4]→S0 transition where O2 is formed and Kok’s water oxidation clock is reset. Our data reveal a complex sequence of events, which occur over micro- to milliseconds, comprising changes at the Mn4CaO5 cluster, its ligands and water pathways as well as controlled proton release through the hydrogen-bonding network of the Cl1 channel. Importantly, the extra O atom Ox, which was introduced as a bridging ligand between Ca and Mn1 during the S2→S3 transition, disappears or relocates in parallel with Yz reduction starting at approximately 700 μs after the third flash. The onset of O2 evolution, as indicated by the shortening of the Mn1–Mn4 distance, occurs at around 1,200 μs, signifying the presence of a reduced intermediate, possibly a bound peroxide.

Place, publisher, year, edition, pages
Springer Nature, 2023
National Category
Biochemistry and Molecular Biology Physical Chemistry
Identifiers
urn:nbn:se:umu:diva-208257 (URN)10.1038/s41586-023-06038-z (DOI)000991687000024 ()37138085 (PubMedID)2-s2.0-85156250364 (Scopus ID)
Funder
Swedish Research Council, 2016-05183Swedish Research Council, 2020-03809Swedish Energy Agency, 45421-1
Note

Errata: Bhowmick, A., Hussein, R., Bogacz, I. et al. Author Correction: Structural evidence for intermediates during O2 formation in photosystem II. Nature (2024). DOI: 10.1038/s41586-024-07099-4

Available from: 2023-05-24 Created: 2023-05-24 Last updated: 2024-02-12Bibliographically approved
Projects
Water-binding and water-splitting by photosystem II and artificial catalysts [2009-03722_VR]; Umeå UniversityTRANSFORMERS - Integrated biomass production using Swedish microorganisms, local wastewaters and flue gases [2015-92_Formas]; Umeå UniversityMechanism and assembly of the water oxidation catalyst in photosystem II [2016-05183_VR]; Umeå UniversityAktivering av basmetaller för elektrokatalytisk vattenspjälkning [P45421-1_Energi]; Uppsala UniversityAmmonia made from Air, Water and Sunshine ‚Äì the ideal renewable fuel [P46551-1_Energi]; Uppsala UniversityRevealing the mechanism of biological water oxidation [2020-03809_VR]; Uppsala University
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0003-2790-7721

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