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Shevela, Dmitriy
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Publications (10 of 26) Show all publications
Shevela, D., Ananyev, G., Vatland, A. K., Arnold, J., Mamedov, F., Eichacker, L. A., . . . Messinger, J. (2019). 'Birth defects' of photosystem II make it highly susceptible to photodamage during chloroplast biogenesis. Physiologia Plantarum: An International Journal for Plant Biology, 166(1), 165-180
Open this publication in new window or tab >>'Birth defects' of photosystem II make it highly susceptible to photodamage during chloroplast biogenesis
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2019 (English)In: Physiologia Plantarum: An International Journal for Plant Biology, ISSN 0031-9317, E-ISSN 1399-3054, Vol. 166, no 1, p. 165-180Article in journal (Refereed) Published
Abstract [en]

High solar flux is known to diminish photosynthetic growth rates, reducing biomass productivity and lowering disease tolerance. Photosystem II (PSII) of plants is susceptible to photodamage (also known as photoinactivation) in strong light, resulting in severe loss of water oxidation capacity and destruction of the water‐oxidizing complex (WOC). The repair of damaged PSIIs comes at a high energy cost and requires de novo biosynthesis of damaged PSII subunits, reassembly of the WOC inorganic cofactors and membrane remodeling. Employing membrane‐inlet mass spectrometry and O2‐polarography under flashing light conditions, we demonstrate that newly synthesized PSII complexes are far more susceptible to photodamage than are mature PSII complexes. We examined these ‘PSII birth defects’ in barley seedlings and plastids (etiochloroplasts and chloroplasts) isolated at various times during de‐etiolation as chloroplast development begins and matures in synchronization with thylakoid membrane biogenesis and grana membrane formation. We show that the degree of PSII photodamage decreases simultaneously with biogenesis of the PSII turnover efficiency measured by O2‐polarography, and with grana membrane stacking, as determined by electron microscopy. Our data from fluorescence, QB‐inhibitor binding, and thermoluminescence studies indicate that the decline of the high‐light susceptibility of PSII to photodamage is coincident with appearance of electron transfer capability QA− → QB during de‐etiolation. This rate depends in turn on the downstream clearing of electrons upon buildup of the complete linear electron transfer chain and the formation of stacked grana membranes capable of longer‐range energy transfer.

Place, publisher, year, edition, pages
Wiley-Blackwell, 2019
Keywords
Practice variation, Bronchopulmonary dysplasia, Preterm infants, Ventilation
National Category
Biophysics
Identifiers
urn:nbn:se:umu:diva-158931 (URN)10.1111/ppl.12932 (DOI)000466108300014 ()30693529 (PubMedID)
Funder
Swedish Research CouncilSwedish Research Council
Note

Special Issue: SI

Available from: 2019-05-15 Created: 2019-05-15 Last updated: 2019-06-10Bibliographically 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)
Available from: 2018-10-15 Created: 2018-10-15 Last updated: 2018-11-09Bibliographically approved
Shevela, D., Björn, L. O. & Govindjee, . (2018). Photosynthesis: solar energy for life. Singapore: World Scientific
Open this publication in new window or tab >>Photosynthesis: solar energy for life
2018 (English)Book (Other academic)
Abstract [en]

Photosynthesis has been an important field of research for more than a century, but the present concerns about energy, environment and climate have greatly intensified interest in and research on this topic. Research has progressed rapidly in recent years, and this book is an interesting read for an audience who is concerned with various ways of harnessing solar energy.

Our understanding of photosynthesis can now be said to have reached encyclopedic dimensions. There have been, in the past, many good books at various levels. Our book is expected to fulfill the needs of advanced undergraduate and beginning graduate students in branches of biology, biochemistry, biophysics, and bioengineering because photosynthesis is the basis of future advances in producing more food, more biomass, more fuel, and new chemicals for our expanding global human population. Further, the basics of photosynthesis are and will be used not only for the above, but in artificial photosynthesis, an important emerging field where chemists, researchers and engineers of solar energy systems will play a major role.

Place, publisher, year, edition, pages
Singapore: World Scientific, 2018. p. 188
National Category
Biological Sciences
Identifiers
urn:nbn:se:umu:diva-153922 (URN)10.1142/10522 (DOI)978-981-3223-10-3 (ISBN)978-981-3223-13-4 (ISBN)
Available from: 2018-12-07 Created: 2018-12-07 Last updated: 2019-04-17Bibliographically approved
Tikhonov, K., Shevela, D., Klimov, V. V. & Messinger, J. (2018). Quantification of bound bicarbonate in photosystem II. Photosynthetica (Praha), 56(1), 210-216
Open this publication in new window or tab >>Quantification of bound bicarbonate in photosystem II
2018 (English)In: Photosynthetica (Praha), ISSN 0300-3604, E-ISSN 1573-9058, Vol. 56, no 1, p. 210-216Article in journal (Refereed) Published
Abstract [en]

In this study, we presented a new approach for quantification of bicarbonate (HCO3-) molecules bound to PSII. Our method, which is based on a combination of membrane-inlet mass spectrometry (MIMS) and O-18-labelling, excludes the possibility of "non-accounted" HCO3- by avoiding (1) the employment of formate for removal of HCO3- from PSII, and (2) the extremely low concentrations of HCO3-/CO2 during online MIMS measurements. By equilibration of PSII sample to ambient CO2 concentration of dissolved CO2/HCO3-, the method ensures that all physiological binding sites are saturated before analysis. With this approach, we determined that in spinach PSII membrane fragments 1.1 +/- 0.1 HCO3- are bound per PSII reaction center, while none was bound to isolated PsbO protein. Our present results confirmed that PSII binds one HCO3- molecule as ligand to the non-heme iron of PSII, while unbound HCO3- optimizes the water-splitting reactions by acting as a mobile proton shuttle.

Keywords
hydrogen carbonate, inorganic carbon, mass spectrometry, Mn-stabilizing protein, non-heme iron, ygen-evolving complex
National Category
Biophysics
Identifiers
urn:nbn:se:umu:diva-147475 (URN)10.1007/s11099-017-0758-4 (DOI)000430309200019 ()
Funder
Swedish Research Council, 2016-05183
Available from: 2018-05-04 Created: 2018-05-04 Last updated: 2018-06-09Bibliographically approved
Kern, J., Chatterjee, R., Young, I. D., Fuller, F. D., Lassalle, L., Ibrahim, M., . . . Yachandra, V. K. (2018). Structures of the intermediates of Kok’s photosynthetic water oxidation clock [Letter to the editor]. Nature, 563, 421-425
Open this publication in new window or tab >>Structures of the intermediates of Kok’s photosynthetic water oxidation clock
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2018 (English)In: Nature, ISSN 0028-0836, E-ISSN 1476-4687, Vol. 563, p. 421-425Article in journal, Letter (Refereed) Published
Abstract [en]

Inspired by the period-four oscillation in flash-induced oxygen evolution of photosystem II discovered by Joliot in 1969, Kok performed additional experiments and proposed a five-state kinetic model for photosynthetic oxygen evolution, known as Kok’s S-state clock or cycle1,2. The model comprises four (meta)stable intermediates (S0, S1, S2 and S3) and one transient S4 state, which precedes dioxygen formation occurring in a concerted reaction from two water-derived oxygens bound at an oxo-bridged tetra manganese calcium (Mn4CaO5) cluster in the oxygen-evolving complex3–7. This reaction is coupled to the two-step reduction and protonation of the mobile plastoquinone QB at the acceptor side of PSII. Here, using serial femtosecond X-ray crystallography and simultaneous X-ray emission spectroscopy with multi-flash visible laser excitation at room temperature, we visualize all (meta)stable states of Kok’s cycle as high-resolution structures (2.04–2.08 Å). In addition, we report structures of two transient states at 150 and 400 µs, revealing notable structural changes including the binding of one additional ‘water’, Ox, during the S2→S3 state transition. Our results suggest that one water ligand to calcium (W3) is directly involved in substrate delivery. The binding of the additional oxygen Ox in the S3 state between Ca and Mn1 supports O–O bond formation mechanisms involving O5 as one substrate, where Ox is either the other substrate oxygen or is perfectly positioned to refill the O5 position during O2 release. Thus, our results exclude peroxo-bond formation in the S3 state, and the nucleophilic attack of W3 onto W2 is unlikely.

Place, publisher, year, edition, pages
Nature Publishing Group, 2018
National Category
Biological Sciences
Identifiers
urn:nbn:se:umu:diva-153920 (URN)10.1038/s41586-018-0681-2 (DOI)000450048400064 ()
Funder
NIH (National Institute of Health), GM055302NIH (National Institute of Health), GM110501NIH (National Institute of Health), GM126289NIH (National Institute of Health), GM117126NIH (National Institute of Health), GM124149NIH (National Institute of Health), GM124169Swedish Research Council, 2016-05183Knut and Alice Wallenberg Foundation, 2011.0055NIH (National Institute of Health), P41GM103393
Available from: 2018-12-07 Created: 2018-12-07 Last updated: 2019-01-14Bibliographically approved
Melder, J., Kwong, W. L., Shevela, D., Messinger, J. & Kurz, P. (2017). Electrocatalytic Water Oxidation by MnOx/C: In Situ Catalyst Formation, Carbon Substrate Variations, and Direct O2/CO2 Monitoring by Membrane-Inlet Mass Spectrometry. ChemSusChem, 10(22), 4491-4502
Open this publication in new window or tab >>Electrocatalytic Water Oxidation by MnOx/C: In Situ Catalyst Formation, Carbon Substrate Variations, and Direct O2/CO2 Monitoring by Membrane-Inlet Mass Spectrometry
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2017 (English)In: ChemSusChem, ISSN 1864-5631, E-ISSN 1864-564X, Vol. 10, no 22, p. 4491-4502Article in journal (Refereed) Published
Abstract [en]

Layers of amorphous manganese oxides were directly formed on the surfaces of different carbon materials by exposing the carbon to aqueous solutions of permanganate (MnO4- ) followed by sintering at 100-400 °C. During electrochemical measurements in neutral aqueous buffer, nearly all of the MnOx /C electrodes show significant oxidation currents at potentials relevant for the oxygen evolution reaction (OER). However, by combining electrolysis with product detection by using mass spectrometry, it was found that these currents were only strictly linked to water oxidation if MnOx was deposited on graphitic carbon materials (faradaic O2 yields >90 %). On the contrary, supports containing sp3 -C were found to be unsuitable as the OER is accompanied by carbon corrosion to CO2 . Thus, choosing the "right" carbon material is crucial for the preparation of stable and efficient MnOx /C anodes for water oxidation catalysis. For MnOx on graphitic substrates, current densities of >1 mA cm-2 at η=540 mV could be maintained for at least 16 h of continuous operation at pH 7 (very good values for electrodes containing only abundant elements such as C, O, and Mn) and post-operando measurements proved the integrity of both the catalyst coating and the underlying carbon at OER conditions.

Place, publisher, year, edition, pages
John Wiley & Sons, 2017
Keywords
carbon materials, electrocatalysis, manganese, mass spectrometry, oxides
National Category
Chemical Sciences
Identifiers
urn:nbn:se:umu:diva-142795 (URN)10.1002/cssc.201701383 (DOI)000416158500025 ()28869720 (PubMedID)
Available from: 2017-12-12 Created: 2017-12-12 Last updated: 2018-06-09Bibliographically approved
Govindjee, ., Shevela, D. & Björn, L. O. (2017). Evolution of the Z-scheme of photosynthesis: a perspective. Paper presented at International Conference on Photosynthesis Research for Sustainability, JUN 19-25, 2016, Pushchino, RUSSIA. Photosynthesis Research, 133(1-3), 5-15
Open this publication in new window or tab >>Evolution of the Z-scheme of photosynthesis: a perspective
2017 (English)In: Photosynthesis Research, ISSN 0166-8595, E-ISSN 1573-5079, Vol. 133, no 1-3, p. 5-15Article in journal (Refereed) Published
Abstract [en]

The concept of the Z-scheme of oxygenic photosynthesis is in all the textbooks. However, its evolution is not. We focus here mainly on some of the history of its biophysical aspects. We have arbitrarily divided here the 1941-2016 period into three sub-periods: (a) Origin of the concept of two light reactions: first hinted at, in 1941, by James Franck and Karl Herzfeld; described and explained, in 1945, by Eugene Rabinowitch; and a clear hypothesis, given in 1956 by Rabinowitch, of the then available cytochrome experiments: one light oxidizing it and another reducing it; (b) Experimental discovery of the two light reactions and two pigment systems and the Z-scheme of photosynthesis: Robert Emerson's discovery, in 1957, of enhancement in photosynthesis when two light beams (one in the far-red region, and the other of shorter wavelengths) are given together than when given separately; and the 1960 scheme of Robin Hill & Fay Bendall; and (c) Evolution of the many versions of the Z-Scheme: Louis Duysens and Jan Amesz's 1961 experiments on oxidation and reduction of cytochrome f by two different wavelengths of light, followed by the work of many others for more than 50 years.

Keywords
Louis N. M. Duysens, Robert Emerson, James Franck, Robin Hill, Bessel Kok, Eugene Rabinowitch, Horst T. Witt, The Z-scheme of photosynthesis
National Category
Botany
Identifiers
urn:nbn:se:umu:diva-137928 (URN)10.1007/s11120-016-0333-z (DOI)000405086400002 ()
Conference
International Conference on Photosynthesis Research for Sustainability, JUN 19-25, 2016, Pushchino, RUSSIA
Available from: 2017-08-04 Created: 2017-08-04 Last updated: 2018-06-09Bibliographically approved
Christianson, H. C., Menard, J. A., Chandran, V. I., Bourseau-Guilmain, E., Shevela, D., Lidfeldt, J., . . . Belting, M. (2017). Tumor antigen glycosaminoglycan modification regulates antibody-drug conjugate delivery and cytotoxicity. OncoTarget, 8(40), 66960-66974
Open this publication in new window or tab >>Tumor antigen glycosaminoglycan modification regulates antibody-drug conjugate delivery and cytotoxicity
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2017 (English)In: OncoTarget, ISSN 1949-2553, E-ISSN 1949-2553, Vol. 8, no 40, p. 66960-66974Article in journal (Refereed) Published
Abstract [en]

Aggressive cancers are characterized by hypoxia, which is a key driver of tumor development and treatment resistance. Proteins specifically expressed in the hypoxic tumor microenvironment thus represent interesting candidates for targeted drug delivery strategies. Carbonic anhydrase (CAIX) has been identified as an attractive treatment target as it is highly hypoxia specific and expressed at the cell-surface to promote cancer cell aggressiveness. Here, we find that cancer cell internalization of CAIX is negatively regulated by post-translational modification with chondroitin or heparan sulfate glycosaminoglycan chains. We show that perturbed glycosaminoglycan modification results in increased CAIX endocytosis. We hypothesized that perturbation of CAIX glycosaminoglycan conjugation may provide opportunities for enhanced drug delivery to hypoxic tumor cells. In support of this concept, pharmacological inhibition of glycosaminoglycan biosynthesis with xylosides significantly potentiated the internalization and cytotoxic activity of an antibody-drug conjugate (ADC) targeted at CAIX. Moreover, cells expressing glycosaminoglycan-deficient CAIX were significantly more sensitive to ADC treatment as compared with cells expressing wild-type CAIX. We find that inhibition of CAIX endocytosis is associated with an increased localization of glycosaminoglycan-conjugated CAIX in membrane lipid raft domains stabilized by caveolin-1 clusters. The association of CAIX with caveolin-1 was partially attenuated by acidosis, i.e. another important feature of malignant tumors. Accordingly, we found increased internalization of CAIX at acidic conditions. These findings provide first evidence that intracellular drug delivery at pathophysiological conditions of malignant tumors can be attenuated by tumor antigen glycosaminoglycan modification, which is of conceptual importance in the future development of targeted cancer treatments.

Place, publisher, year, edition, pages
IMPACT JOURNALS LLC, 2017
Keywords
tumor antigen, glycosylation, hypoxia, immunotherapy, proteoglycan
National Category
Cancer and Oncology
Identifiers
urn:nbn:se:umu:diva-140464 (URN)10.18632/oncotarget.16921 (DOI)000410790500017 ()
Available from: 2017-10-25 Created: 2017-10-25 Last updated: 2018-06-09Bibliographically approved
Shevela, D., Arnold, J., Reisinger, V., Berends, H.-M., Kmiec, K., Koroidov, S., . . . Eichacker, L. A. (2016). Biogenesis of water splitting by photosystem II during de-etiolation of barley (Hordeum vulgare L.). Plant, Cell and Environment, 39(7), 1524-1536
Open this publication in new window or tab >>Biogenesis of water splitting by photosystem II during de-etiolation of barley (Hordeum vulgare L.)
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2016 (English)In: Plant, Cell and Environment, ISSN 0140-7791, E-ISSN 1365-3040, Vol. 39, no 7, p. 1524-1536Article in journal (Refereed) Published
Abstract [en]

Etioplasts lack thylakoid membranes and photosystem complexes. Light triggers differentiation of etioplasts into mature chloroplasts, and photosystem complexes assemble in parallel with thylakoid membrane development. Plastids isolated at various time points of de-etiolation are ideal to study the kinetic biogenesis of photosystem complexes during chloroplast development. Here, we investigated the chronology of photosystem II (PSII) biogenesis by monitoring assembly status of chlorophyll-binding protein complexes and development of water splitting via O2 production in plastids (etiochloroplasts) isolated during de-etiolation of barley (Hordeum vulgare L.). Assembly of PSII monomers, dimers and complexes binding outer light-harvesting antenna [PSII-light-harvesting complex II (LHCII) supercomplexes] was identified after 1, 2 and 4 h of de-etiolation, respectively. Water splitting was detected in parallel with assembly of PSII monomers, and its development correlated with an increase of bound Mn in the samples. After 4 h of de-etiolation, etiochloroplasts revealed the same water-splitting efficiency as mature chloroplasts. We conclude that the capability of PSII to split water during de-etiolation precedes assembly of the PSII-LHCII supercomplexes. Taken together, data show a rapid establishment of water-splitting activity during etioplast-to-chloroplast transition and emphasize that assembly of the functional water-splitting site of PSII is not the rate-limiting step in the formation of photoactive thylakoid membranes.

Place, publisher, year, edition, pages
John Wiley & Sons, 2016
Keywords
chloroplast biogenesis, oxygen evolution, oxygen-evolving complex, photosystem II assembly
National Category
Chemical Sciences Botany
Identifiers
urn:nbn:se:umu:diva-123557 (URN)10.1111/pce.12719 (DOI)000381496900012 ()26836813 (PubMedID)
External cooperation:
Available from: 2016-07-06 Created: 2016-07-06 Last updated: 2018-06-07Bibliographically approved
Young, I. D., Ibrahim, M., Chatterjee, R., Gul, S., Fuller, F. D., Koroidov, S., . . . Yano, J. (2016). Structure of photosystem II and substrate binding at room temperature. Nature, 540(7633), 453-457
Open this publication in new window or tab >>Structure of photosystem II and substrate binding at room temperature
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2016 (English)In: Nature, ISSN 0028-0836, E-ISSN 1476-4687, Vol. 540, no 7633, p. 453-457Article in journal (Refereed) Published
Abstract [en]

Light-induced oxidation of water by photosystem II (PS II) in plants, algae and cyanobacteria has generated most of the dioxygen in the atmosphere. PS II, a membrane-bound multi-subunit pigment protein complex, couples the one-electron photochemistry at the reaction centre with the four-electron redox chemistry of water oxidation at the Mn4CaO5 cluster in the oxygen-evolving complex (OEC). Under illumination, the OEC cycles through five intermediate S-states (S0 to S4)1, in which S1 is the dark-stable state and S3 is the last semi-stable state before O–O bond formation and O2 evolution2,3. A detailed understanding of the O–O bond formation mechanism remains a challenge, and will require elucidation of both the structures of the OEC in the different S-states and the binding of the two substrate waters to the catalytic site4–6. Here we report the use of femtosecond pulses from an X-ray free electron laser (XFEL) to obtain damage-free, room temperature structures of dark-adapted (S1), two-flash illuminated (2F; S3-enriched), and ammonia-bound two-flash illuminated (2F-NH3; S3-enriched) PS II. Although the recent 1.95 Å resolution structure of PS II at cryogenic temperature using an XFEL7 provided a damage-free view of the S1 state, measurements at room temperature are required to study the structural landscape of proteins under functional conditions8,9, and also for in situ advancement of the S-states. To investigate the water-binding site(s), ammonia, a water analogue, has been used as a marker, as it binds to the Mn4CaO5 cluster in the S2 and S3 states10. Since the ammonia-bound OEC is active, the ammonia-binding Mn site is not a substrate water site10–13. This approach, together with a comparison of the native dark and 2F states, is used to discriminate between proposed O–O bond formation mechanisms.

Place, publisher, year, edition, pages
Macmillan Publishers Ltd., 2016
National Category
Chemical Sciences
Identifiers
urn:nbn:se:umu:diva-128748 (URN)10.1038/nature20161 (DOI)000389716800046 ()27871088 (PubMedID)
Available from: 2016-12-14 Created: 2016-12-14 Last updated: 2018-06-09Bibliographically approved
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