L-Edge X-ray Absorption Spectroscopy of Dilute Systems Relevant to Metalloproteins Using an X-ray Free-Electron Laser. Mitzner, R., Rehanek, J., Kern, J., Gul, S., Hattne, J., Taguchi, T., Alonso-Mori, R., Tran, R., Weniger, C., Schröder, H., Quevedo, W., Laksmono, H., Sierra, R. G., Han, G., Lassalle-Kaiser, B., Koroidov, S., Kubicek, K., Schreck, S., Kunnus, K., Brzhezinskaya, M., Firsov, A., Minitti, M. P., Turner, J. J., Moeller, S., Sauter, N. K., Bogan, M. J., Nordlund, D., Schlotter, W. F., Messinger, J., Borovik, A., Techert, S., de Groot, F. M. F., Föhlisch, A., Erko, A., Bergmann, U., Yachandra, V. K., Wernet, P., & Yano, J. The Journal of Physical Chemistry Letters, 4(21):3641–3647, November, 2013. Publisher: American Chemical Society
L-Edge X-ray Absorption Spectroscopy of Dilute Systems Relevant to Metalloproteins Using an X-ray Free-Electron Laser [link]Paper  doi  abstract   bibtex   
L-edge spectroscopy of 3d transition metals provides important electronic structure information and has been used in many fields. However, the use of this method for studying dilute aqueous systems, such as metalloenzymes, has not been prevalent because of severe radiation damage and the lack of suitable detection systems. Here we present spectra from a dilute Mn aqueous solution using a high-transmission zone-plate spectrometer at the Linac Coherent Light Source (LCLS). The spectrometer has been optimized for discriminating the Mn L-edge signal from the overwhelming O K-edge background that arises from water and protein itself, and the ultrashort LCLS X-ray pulses can outrun X-ray induced damage. We show that the deviations of the partial-fluorescence yield-detected spectra from the true absorption can be well modeled using the state-dependence of the fluorescence yield, and discuss implications for the application of our concept to biological samples.
@article{mitzner_l-edge_2013,
	title = {L-{Edge} {X}-ray {Absorption} {Spectroscopy} of {Dilute} {Systems} {Relevant} to {Metalloproteins} {Using} an {X}-ray {Free}-{Electron} {Laser}},
	volume = {4},
	url = {https://doi.org/10.1021/jz401837f},
	doi = {10.1021/jz401837f},
	abstract = {L-edge spectroscopy of 3d transition metals provides important electronic structure information and has been used in many fields. However, the use of this method for studying dilute aqueous systems, such as metalloenzymes, has not been prevalent because of severe radiation damage and the lack of suitable detection systems. Here we present spectra from a dilute Mn aqueous solution using a high-transmission zone-plate spectrometer at the Linac Coherent Light Source (LCLS). The spectrometer has been optimized for discriminating the Mn L-edge signal from the overwhelming O K-edge background that arises from water and protein itself, and the ultrashort LCLS X-ray pulses can outrun X-ray induced damage. We show that the deviations of the partial-fluorescence yield-detected spectra from the true absorption can be well modeled using the state-dependence of the fluorescence yield, and discuss implications for the application of our concept to biological samples.},
	number = {21},
	urldate = {2024-12-10},
	journal = {The Journal of Physical Chemistry Letters},
	author = {Mitzner, Rolf and Rehanek, Jens and Kern, Jan and Gul, Sheraz and Hattne, Johan and Taguchi, Taketo and Alonso-Mori, Roberto and Tran, Rosalie and Weniger, Christian and Schröder, Henning and Quevedo, Wilson and Laksmono, Hartawan and Sierra, Raymond G. and Han, Guangye and Lassalle-Kaiser, Benedikt and Koroidov, Sergey and Kubicek, Katharina and Schreck, Simon and Kunnus, Kristjan and Brzhezinskaya, Maria and Firsov, Alexander and Minitti, Michael P. and Turner, Joshua J. and Moeller, Stefan and Sauter, Nicholas K. and Bogan, Michael J. and Nordlund, Dennis and Schlotter, William F. and Messinger, Johannes and Borovik, Andrew and Techert, Simone and de Groot, Frank M. F. and Föhlisch, Alexander and Erko, Alexei and Bergmann, Uwe and Yachandra, Vittal K. and Wernet, Philippe and Yano, Junko},
	month = nov,
	year = {2013},
	note = {Publisher: American Chemical Society},
	pages = {3641--3647},
}

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