Assignment of the slowly exchanging substrate water of nature’s water-splitting cofactor. de Lichtenberg, C., Rapatskiy, L., Reus, M., Heyno, E., Schnegg, A., Nowaczyk, M. M., Lubitz, W., Messinger, J., & Cox, N. Proceedings of the National Academy of Sciences, 121(11):e2319374121, March, 2024. Publisher: Proceedings of the National Academy of Sciences![Assignment of the slowly exchanging substrate water of nature’s water-splitting cofactor [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex 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.
@article{de_lichtenberg_assignment_2024,
title = {Assignment of the slowly exchanging substrate water of nature’s water-splitting cofactor},
volume = {121},
url = {https://www.pnas.org/doi/full/10.1073/pnas.2319374121},
doi = {10.1073/pnas.2319374121},
abstract = {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.},
number = {11},
urldate = {2024-10-16},
journal = {Proceedings of the National Academy of Sciences},
author = {de Lichtenberg, Casper and Rapatskiy, Leonid and Reus, Michael and Heyno, Eiri and Schnegg, Alexander and Nowaczyk, Marc M. and Lubitz, Wolfgang and Messinger, Johannes and Cox, Nicholas},
month = mar,
year = {2024},
note = {Publisher: Proceedings of the National Academy of Sciences},
pages = {e2319374121},
}
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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. 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