“Invisible” detergents enable a reliable determination of solution structures of native photosystems by small-angle neutron scattering
dc.contributor.author | Golub, M | en_AU |
dc.contributor.author | Gätcke, J | en_AU |
dc.contributor.author | Subramanian, S | en_AU |
dc.contributor.author | Kölsch, A | en_AU |
dc.contributor.author | Darwish, TA | en_AU |
dc.contributor.author | Feoktystov, A | en_AU |
dc.contributor.author | Matsarskaia, O | en_AU |
dc.contributor.author | Martel, A | en_AU |
dc.contributor.author | Porcar, L | en_AU |
dc.contributor.author | Zouni, A | en_AU |
dc.contributor.author | Pieper, J | en_AU |
dc.date.accessioned | 2023-11-30T22:13:38Z | en_AU |
dc.date.available | 2023-11-30T22:13:38Z | en_AU |
dc.date.issued | 2022-04-06 | en_AU |
dc.date.statistics | 2022-05-06 | en_AU |
dc.description.abstract | Photosystems I (PSI) and II (PSII) are pigment–protein complexes capable of performing the light-induced charge separation necessary to convert solar energy into a biochemically storable form, an essential step in photosynthesis. Small-angle neutron scattering (SANS) is unique in providing structural information on PSI and PSII in solution under nearly physiological conditions without the need for crystallization or temperature decrease. We show that the reliability of the solution structure critically depends on proper contrast matching of the detergent belt surrounding the protein. Especially, specifically deuterated (“invisible”) detergents are shown to be properly matched out in SANS experiments by a direct, quantitative comparison with conventional matching strategies. In contrast, protonated detergents necessarily exhibit incomplete matching so that related SANS results systematically overestimate the size of the membrane protein under study. While the solution structures obtained are close to corresponding high-resolution structures, we show that temperature and solution state lead to individual structural differences compared with high-resolution structures. We attribute these differences to the presence of a manifold of conformational substates accessible by protein dynamics under physiological conditions. © 2022 American Chemical Society | en_AU |
dc.description.sponsorship | Financial support by the Estonian Research Council (Grants PRG 539 and SLOKT 12026 T) is gratefully acknowledged. This work was also partly financed by the Baltic-German University Liaison Office supported by the German Academic Exchange Service (DAAD) with funds from the Foreign Office of the Federal Republic of Germany. A.Z. is grateful for financial support by Germany’s Excellence Strategy Project EXC 2008/1-390540038 (A.Z.) coordinated by T.U. Berlin and by the German Research Foundation (DFG) via the Collaborative Research Center SFB1078 (Humboldt Universität zu Berlin), TP A5 (A.Z., J.G.) and for the support by the Bundesministerium für Bildung und Forschung, Germany, 2020, projects 031B0557 A+B (A.K., A.Z., and S.S.). The authors also thank the ILL (Grenoble, France) for the allocation of beamtime at the SANS instrument D22 and the Jülich Centre for Neutron Science (JCNS) at the Heinz Maier-Leibnitz Zentrum MLZ (Garching, Germany) for beamtime at the KWS-1 SANS instrument. The ILL SANS data are permanently curated by the ILL and accessible via the DOI 10.5291/ILL-DATA.TEST-3114. Finally, the authors are very grateful to the National Deuteration Facility, Australian Nuclear Science and Technology Organization ANSTO (Lucas Heights, Australia) for providing the deuterated detergent used in our experiments. The National Deuteration Facility is partly supported by the National Collaborative Research Infrastructure Strategy─an initiative of the Australian Government. | en_AU |
dc.identifier.citation | Golub, M., Gätcke, J., Subramanian, S., Kölsch, A., Darwish, T., Howard, J. K., Feoktystov, A., Matsarskaia, O., Martel, A., Porcar, L., Zouni, A., & Pieper, J. (2022). “Invisible” detergents enable a reliable determination of solution structures of native photosystems by small-angle neutron scattering. The Journal of Physical Chemistry B, 126(15), 2824-2833. doi:10.1021/acs.jpcb.2c01591 | en_AU |
dc.identifier.issn | 1520-6106 | en_AU |
dc.identifier.issue | 15 | en_AU |
dc.identifier.journaltitle | The Journal of Physical Chemistry B | en_AU |
dc.identifier.pagination | 2824-2833 | en_AU |
dc.identifier.uri | https://doi.org/10.1021/acs.jpcb.2c01591 | en_AU |
dc.identifier.uri | https://apo.ansto.gov.au/handle/10238/15253 | en_AU |
dc.identifier.volume | 126 | en_AU |
dc.language.iso | en | en_AU |
dc.publisher | ACS Publications | en_AU |
dc.relation.uri | https://doi.org/10.1021/acs.jpcb.2c01591 | en_AU |
dc.subject | Detergents | en_AU |
dc.subject | Solutions | en_AU |
dc.subject | Small angle scattering | en_AU |
dc.subject | Energy storage | en_AU |
dc.subject | Proteins | en_AU |
dc.subject | Solar energy | en_AU |
dc.title | “Invisible” detergents enable a reliable determination of solution structures of native photosystems by small-angle neutron scattering | en_AU |
dc.type | Journal Article | en_AU |
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