Room temperature X-ray absorption spectroscopy of metalloenzymes with drop-on-demand sample delivery at XFELs

Isabel Bogacz; Hiroki Makita; Philipp S. Simon; Miao Zhang; Margaret D. Doyle; Ruchira Chatterjee; Thomas Fransson; Clemens Weninger; Franklin Fuller; Leland Gee; Takahiro Sato; Matthew Seaberg; Roberto Alonso-Mori; Uwe Bergmann; Vittal K. Yachandra; Jan Kern; Junko Yano

doi:10.1515/pac-2023-0213

Room temperature X-ray absorption spectroscopy of metalloenzymes with drop-on-demand sample delivery at XFELs

Isabel Bogacz, Hiroki Makita, Philipp S. Simon, Miao Zhang, Margaret D. Doyle, Ruchira Chatterjee, Thomas Fransson, Clemens Weninger, Franklin Fuller, Leland Gee, Takahiro Sato, Matthew Seaberg, Roberto Alonso-Mori, Uwe Bergmann, Vittal K. Yachandra, Jan Kern, Junko Yano

Research output: Contribution to journal › Article › peer-review

Abstract

X-ray crystallography and X-ray spectroscopy using X-ray free electron lasers plays an important role in understanding the interplay of structural changes in the protein and the chemical changes at the metal active site of metalloenzymes through their catalytic cycles. As a part of such an effort, we report here our recent development of methods for X-ray absorption spectroscopy (XAS) at XFELs to study dilute biological samples, available in limited volumes. Our prime target is Photosystem II (PS II), a multi subunit membrane protein complex, that catalyzes the light-driven water oxidation reaction at the Mn4CaO5 cluster. This is an ideal system to investigate how to control multi-electron/proton chemistry, using the flexibility of metal redox states, in coordination with the protein and the water network. We describe the method that we have developed to collect XAS data using PS II samples with a Mn concentration of <1 mM, using a drop-on-demand sample delivery method.

Original language	English
Pages (from-to)	891-897
Journal	Pure and Applied Chemistry
Volume	95
Issue number	8
Early online date	2023
DOIs	https://doi.org/10.1515/pac-2023-0213
Publication status	Published - 2023

Subject classification (UKÄ)

Biological Sciences
Biophysics

Free keywords

Manganese
photoiupac 2022
photosystem II
water oxidation
X-ray absorption spectroscopy
X-ray free electron lasers

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10.1515/pac-2023-0213

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Bogacz, I., Makita, H., Simon, P. S., Zhang, M., Doyle, M. D., Chatterjee, R., Fransson, T., Weninger, C., Fuller, F., Gee, L., Sato, T., Seaberg, M., Alonso-Mori, R., Bergmann, U., Yachandra, V. K., Kern, J., & Yano, J. (2023). Room temperature X-ray absorption spectroscopy of metalloenzymes with drop-on-demand sample delivery at XFELs. Pure and Applied Chemistry, 95(8), 891-897. https://doi.org/10.1515/pac-2023-0213

@article{e11aa756146b4641b7116d83f263efdf,

title = "Room temperature X-ray absorption spectroscopy of metalloenzymes with drop-on-demand sample delivery at XFELs",

abstract = "X-ray crystallography and X-ray spectroscopy using X-ray free electron lasers plays an important role in understanding the interplay of structural changes in the protein and the chemical changes at the metal active site of metalloenzymes through their catalytic cycles. As a part of such an effort, we report here our recent development of methods for X-ray absorption spectroscopy (XAS) at XFELs to study dilute biological samples, available in limited volumes. Our prime target is Photosystem II (PS II), a multi subunit membrane protein complex, that catalyzes the light-driven water oxidation reaction at the Mn4CaO5 cluster. This is an ideal system to investigate how to control multi-electron/proton chemistry, using the flexibility of metal redox states, in coordination with the protein and the water network. We describe the method that we have developed to collect XAS data using PS II samples with a Mn concentration of <1 mM, using a drop-on-demand sample delivery method.",

keywords = "Manganese, photoiupac 2022, photosystem II, water oxidation, X-ray absorption spectroscopy, X-ray free electron lasers",

author = "Isabel Bogacz and Hiroki Makita and Simon, {Philipp S.} and Miao Zhang and Doyle, {Margaret D.} and Ruchira Chatterjee and Thomas Fransson and Clemens Weninger and Franklin Fuller and Leland Gee and Takahiro Sato and Matthew Seaberg and Roberto Alonso-Mori and Uwe Bergmann and Yachandra, {Vittal K.} and Jan Kern and Junko Yano",

year = "2023",

doi = "10.1515/pac-2023-0213",

language = "English",

volume = "95",

pages = "891--897",

journal = "Pure and Applied Chemistry",

issn = "0033-4545",

publisher = "De Gruyter",

number = "8",

}

Bogacz, I, Makita, H, Simon, PS, Zhang, M, Doyle, MD, Chatterjee, R, Fransson, T, Weninger, C, Fuller, F, Gee, L, Sato, T, Seaberg, M, Alonso-Mori, R, Bergmann, U, Yachandra, VK, Kern, J & Yano, J 2023, 'Room temperature X-ray absorption spectroscopy of metalloenzymes with drop-on-demand sample delivery at XFELs', Pure and Applied Chemistry, vol. 95, no. 8, pp. 891-897. https://doi.org/10.1515/pac-2023-0213

TY - JOUR

T1 - Room temperature X-ray absorption spectroscopy of metalloenzymes with drop-on-demand sample delivery at XFELs

AU - Bogacz, Isabel

AU - Makita, Hiroki

AU - Simon, Philipp S.

AU - Zhang, Miao

AU - Doyle, Margaret D.

AU - Chatterjee, Ruchira

AU - Fransson, Thomas

AU - Weninger, Clemens

AU - Fuller, Franklin

AU - Gee, Leland

AU - Sato, Takahiro

AU - Seaberg, Matthew

AU - Alonso-Mori, Roberto

AU - Bergmann, Uwe

AU - Yachandra, Vittal K.

AU - Kern, Jan

AU - Yano, Junko

PY - 2023

Y1 - 2023

N2 - X-ray crystallography and X-ray spectroscopy using X-ray free electron lasers plays an important role in understanding the interplay of structural changes in the protein and the chemical changes at the metal active site of metalloenzymes through their catalytic cycles. As a part of such an effort, we report here our recent development of methods for X-ray absorption spectroscopy (XAS) at XFELs to study dilute biological samples, available in limited volumes. Our prime target is Photosystem II (PS II), a multi subunit membrane protein complex, that catalyzes the light-driven water oxidation reaction at the Mn4CaO5 cluster. This is an ideal system to investigate how to control multi-electron/proton chemistry, using the flexibility of metal redox states, in coordination with the protein and the water network. We describe the method that we have developed to collect XAS data using PS II samples with a Mn concentration of <1 mM, using a drop-on-demand sample delivery method.

AB - X-ray crystallography and X-ray spectroscopy using X-ray free electron lasers plays an important role in understanding the interplay of structural changes in the protein and the chemical changes at the metal active site of metalloenzymes through their catalytic cycles. As a part of such an effort, we report here our recent development of methods for X-ray absorption spectroscopy (XAS) at XFELs to study dilute biological samples, available in limited volumes. Our prime target is Photosystem II (PS II), a multi subunit membrane protein complex, that catalyzes the light-driven water oxidation reaction at the Mn4CaO5 cluster. This is an ideal system to investigate how to control multi-electron/proton chemistry, using the flexibility of metal redox states, in coordination with the protein and the water network. We describe the method that we have developed to collect XAS data using PS II samples with a Mn concentration of <1 mM, using a drop-on-demand sample delivery method.

KW - Manganese

KW - photoiupac 2022

KW - photosystem II

KW - water oxidation

KW - X-ray absorption spectroscopy

KW - X-ray free electron lasers

U2 - 10.1515/pac-2023-0213

DO - 10.1515/pac-2023-0213

M3 - Article

C2 - 38013689

AN - SCOPUS:85153478031

SN - 0033-4545

VL - 95

SP - 891

EP - 897

JO - Pure and Applied Chemistry

JF - Pure and Applied Chemistry

IS - 8

ER -

Room temperature X-ray absorption spectroscopy of metalloenzymes with drop-on-demand sample delivery at XFELs

Abstract

Subject classification (UKÄ)

Free keywords

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