{"entity": "researcher", "timestamp": "2026-07-22T17:17:05.011Z", "family": "Shutova", "given": "Tatyana", "initials": "T", "orcid": "0000-0002-4095-9609", "affiliations": ["Department of Plant PhysiologyUme\u00e5 University Ume\u00e5 SE\u2010907 36, Sweden"], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/ec5a10e3ad274526b819f24961ab015e.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/ec5a10e3ad274526b819f24961ab015e"}}, "publications": [{"entity": "publication", "iuid": "2a6a88ecb8924b3cb97256b268e8c722", "links": {"self": {"href": "https://publications.scilifelab.se/publication/2a6a88ecb8924b3cb97256b268e8c722.json"}, "display": {"href": "https://publications.scilifelab.se/publication/2a6a88ecb8924b3cb97256b268e8c722"}}, "title": "Direct energy transfer from photosystem II to photosystem I confers winter sustainability in Scots Pine.", "authors": [{"family": "Bag", "given": "Pushan", "initials": "P", "orcid": "0000-0003-3858-4606", "researcher": {"href": "https://publications.scilifelab.se/researcher/033b97dc712047a294d3e801ba750787.json"}}, {"family": "Chukhutsina", "given": "Volha", "initials": "V"}, {"family": "Zhang", "given": "Zishan", "initials": "Z"}, {"family": "Paul", "given": "Suman", "initials": "S"}, {"family": "Ivanov", "given": "Alexander G", "initials": "AG", "orcid": "0000-0001-7910-5494", "researcher": {"href": "https://publications.scilifelab.se/researcher/1cc5e19a40374d67a3ae74182c5dae6f.json"}}, {"family": "Shutova", "given": "Tatyana", "initials": "T", "orcid": "0000-0002-4095-9609", "researcher": {"href": "https://publications.scilifelab.se/researcher/ec5a10e3ad274526b819f24961ab015e.json"}}, {"family": "Croce", "given": "Roberta", "initials": "R", "orcid": "0000-0003-3469-834X", "researcher": {"href": "https://publications.scilifelab.se/researcher/119277ddfe3b4e9ab4e9afc972f5e763.json"}}, {"family": "Holzwarth", "given": "Alfred R", "initials": "AR", "orcid": "0000-0002-9562-4873", "researcher": {"href": "https://publications.scilifelab.se/researcher/40ce08a698124e0f888d3db0a0644162.json"}}, {"family": "Jansson", "given": "Stefan", "initials": "S", "orcid": "0000-0002-7906-6891", "researcher": {"href": "https://publications.scilifelab.se/researcher/fb9d3c17f4514903b3731d15c622a53d.json"}}], "type": "journal article", "published": "2020-12-15", "journal": {"title": "Nat Commun", "issn": "2041-1723", "issn-l": "2041-1723", "volume": "11", "issue": "1", "pages": "6388"}, "abstract": "Evergreen conifers in boreal forests can survive extremely cold (freezing) temperatures during long dark winter and fully recover during summer. A phenomenon called \"sustained quenching\" putatively provides photoprotection and enables their survival, but its precise molecular and physiological mechanisms are not understood. To unveil them, here we have analyzed seasonal adjustment of the photosynthetic machinery of Scots pine (Pinus sylvestris) trees by monitoring multi-year changes in weather, chlorophyll fluorescence, chloroplast ultrastructure, and changes in pigment-protein composition. Analysis of Photosystem II and Photosystem I performance parameters indicate that highly dynamic structural and functional seasonal rearrangements of the photosynthetic apparatus occur. Although several mechanisms might contribute to 'sustained quenching' of winter/early spring pine needles, time-resolved fluorescence analysis shows that extreme down-regulation of photosystem II activity along with direct energy transfer from photosystem II to photosystem I play a major role. This mechanism is enabled by extensive thylakoid destacking allowing for the mixing of PSII with PSI complexes. These two linked phenomena play crucial roles in winter acclimation and protection.", "doi": "10.1038/s41467-020-20137-9", "pmid": "33319777", "labels": {"Integrated Microscopy Technologies Ume\u00e5": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC7738668"}, {"db": "pii", "key": "10.1038/s41467-020-20137-9"}], "notes": [], "created": "2022-04-01T15:00:18.942Z", "modified": "2023-06-19T12:41:41.017Z"}, {"entity": "publication", "iuid": "10971b3610c243aaaf7fe9b336cc58a2", "links": {"self": {"href": "https://publications.scilifelab.se/publication/10971b3610c243aaaf7fe9b336cc58a2.json"}, "display": {"href": "https://publications.scilifelab.se/publication/10971b3610c243aaaf7fe9b336cc58a2"}}, "title": "Dynamic pH-induced conformational changes of the PsbO protein in the fluctuating acidity of the thylakoid lumen.", "authors": [{"family": "Carius", "given": "Anke B", "initials": "AB"}, {"family": "Rogne", "given": "Per", "initials": "P"}, {"family": "Duchoslav", "given": "Milo\u0161", "initials": "M"}, {"family": "Wolf-Watz", "given": "Magnus", "initials": "M"}, {"family": "Samuelsson", "given": "G\u00f6ran", "initials": "G"}, {"family": "Shutova", "given": "Tatyana", "initials": "T", "orcid": "0000-0002-4095-9609", "researcher": {"href": "https://publications.scilifelab.se/researcher/ec5a10e3ad274526b819f24961ab015e.json"}}], "type": "journal article", "published": "2019-05-00", "journal": {"title": "Physiol Plantarum", "issn": "1399-3054", "volume": "166", "issue": "1", "pages": "288-299", "issn-l": "0031-9317"}, "abstract": "The PsbO protein is an essential extrinsic subunit of photosystem II, the pigment-protein complex responsible for light-driven water splitting. Water oxidation in photosystem II supplies electrons to the photosynthetic electron transfer chain and is accompanied by proton release and oxygen evolution. While the electron transfer steps in this process are well defined and characterized, the driving forces acting on the liberated protons, their dynamics and their destiny are all largely unknown. It was suggested that PsbO undergoes proton-induced conformational changes and forms hydrogen bond networks that ensure prompt proton removal from the catalytic site of water oxidation, i.e. the Mn 4 CaO5 cluster. This work reports the purification and characterization of heterologously expressed PsbO from green algae Chlamydomonas reinhardtii and two isoforms from the higher plant Solanum tuberosum (PsbO1 and PsbO2). A comparison to the spinach PsbO reveals striking similarities in intrinsic protein fluorescence and CD spectra, reflecting the near-identical secondary structure of the proteins from algae and higher plants. Titration experiments using the hydrophobic fluorescence probe ANS revealed that eukaryotic PsbO proteins exhibit acid-base hysteresis. This hysteresis is a dynamic effect accompanied by changes in the accessibility of the protein's hydrophobic core and is not due to reversible oligomerization or unfolding of the PsbO protein. These results confirm the hypothesis that pH-dependent dynamic behavior at physiological pH ranges is a common feature of PsbO proteins and causes reversible opening and closing of their \u03b2-barrel domain in response to the fluctuating acidity of the thylakoid lumen.", "doi": "10.1111/ppl.12948", "pmid": "30793329", "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [], "notes": [], "created": "2019-12-20T16:14:55.880Z", "modified": "2025-10-17T13:03:57.950Z"}]}