X-ray Absorption Spectroscopy of Dilute Metalloenzymes at X-ray Free-Electron Lasers in a Shot-by-Shot Mode. Bogacz, I., Szilagyi, E., Makita, H., Simon, P. S., Zhang, M., Doyle, M. D., Chatterjee, K., Kretzschmar, M., Chernev, P., Croy, N., Cheah, M., Dasgupta, M., Nangca, I., Fransson, T., Bhowmick, A., Brewster, A. S., Sauter, N. K., Owada, S., Tono, K., Zerdane, S., Oggenfuss, A., Babich, D., Sander, M., Mankowsky, R., Lemke, H. T., Gee, L. B., Sato, T., Kroll, T., Messinger, J., Alonso-Mori, R., Bergmann, U., Sokaras, D., Yachandra, V. K., Kern, J., & Yano, J. The Journal of Physical Chemistry Letters, 16(15):3778–3787, April, 2025. Publisher: American Chemical Society![X-ray Absorption Spectroscopy of Dilute Metalloenzymes at X-ray Free-Electron Lasers in a Shot-by-Shot Mode [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex X-ray absorption spectroscopy (XAS) of 3d transition metals provides important electronic structure information for many fields. However, X-ray-induced radiation damage under physiological temperature has prevented using this method to study dilute aqueous systems, such as metalloenzymes, as the catalytic reaction proceeds. Here we present a new approach to enable operando XAS of dilute biological samples and demonstrate its feasibility with K-edge XAS spectra from the Mn cluster in photosystem II and the Fe–S centers in photosystem I. This approach combines highly efficient sample delivery strategies and a robust signal normalization method with high-transmission Bragg diffraction-based spectrometers at X-ray free-electron lasers (XFELs) in a damage-free, shot-by-shot mode. These photon-out spectrometers have been optimized for discriminating the metal Mn/Fe Kα fluorescence signals from the overwhelming scattering background present on currently available detectors for XFELs that lack suitable energy discrimination. We quantify the enhanced performance metrics of the spectrometer and discuss its potential applications for acquiring time-resolved XAS spectra of biological samples during their reactions at XFELs.
@article{bogacz_x-ray_2025,
title = {X-ray {Absorption} {Spectroscopy} of {Dilute} {Metalloenzymes} at {X}-ray {Free}-{Electron} {Lasers} in a {Shot}-by-{Shot} {Mode}},
volume = {16},
url = {https://doi.org/10.1021/acs.jpclett.5c00399},
doi = {10.1021/acs.jpclett.5c00399},
abstract = {X-ray absorption spectroscopy (XAS) of 3d transition metals provides important electronic structure information for many fields. However, X-ray-induced radiation damage under physiological temperature has prevented using this method to study dilute aqueous systems, such as metalloenzymes, as the catalytic reaction proceeds. Here we present a new approach to enable operando XAS of dilute biological samples and demonstrate its feasibility with K-edge XAS spectra from the Mn cluster in photosystem II and the Fe–S centers in photosystem I. This approach combines highly efficient sample delivery strategies and a robust signal normalization method with high-transmission Bragg diffraction-based spectrometers at X-ray free-electron lasers (XFELs) in a damage-free, shot-by-shot mode. These photon-out spectrometers have been optimized for discriminating the metal Mn/Fe Kα fluorescence signals from the overwhelming scattering background present on currently available detectors for XFELs that lack suitable energy discrimination. We quantify the enhanced performance metrics of the spectrometer and discuss its potential applications for acquiring time-resolved XAS spectra of biological samples during their reactions at XFELs.},
number = {15},
urldate = {2025-04-22},
journal = {The Journal of Physical Chemistry Letters},
author = {Bogacz, Isabel and Szilagyi, Erzsi and Makita, Hiroki and Simon, Philipp S. and Zhang, Miao and Doyle, Margaret D. and Chatterjee, Kuntal and Kretzschmar, Moritz and Chernev, Petko and Croy, Nicholas and Cheah, Mun-Hon and Dasgupta, Medhanjali and Nangca, Isabela and Fransson, Thomas and Bhowmick, Asmit and Brewster, Aaron S. and Sauter, Nicholas K. and Owada, Shigeki and Tono, Kensuke and Zerdane, Serhane and Oggenfuss, Alexander and Babich, Danylo and Sander, Mathias and Mankowsky, Roman and Lemke, Henrik T. and Gee, Leland B. and Sato, Takahiro and Kroll, Thomas and Messinger, Johannes and Alonso-Mori, Roberto and Bergmann, Uwe and Sokaras, Dimosthenis and Yachandra, Vittal K. and Kern, Jan and Yano, Junko},
month = apr,
year = {2025},
note = {Publisher: American Chemical Society},
pages = {3778--3787},
}
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