Structure and Orientation of the Mn4Ca Cluster in Plant Photosystem II Membranes Studied by Polarized Range-extended X-ray Absorption Spectroscopy*♦. Pushkar, Y., Yano, J., Glatzel, P., Messinger, J., Lewis, A., Sauer, K., Bergmann, U., & Yachandra, V. Journal of Biological Chemistry, 282(10):7198–7208, March, 2007. ![Structure and Orientation of the Mn4Ca Cluster in Plant Photosystem II Membranes Studied by Polarized Range-extended X-ray Absorption Spectroscopy*♦ [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex X-ray absorption spectroscopy has provided important insights into the structure and function of the Mn4Ca cluster in the oxygen-evolving complex of Photosystem II (PS II). The range of manganese extended x-ray absorption fine structure data collected from PS II until now has been, however, limited by the presence of iron in PS II. Using a crystal spectrometer with high energy resolution to detect solely the manganese Kα fluorescence, we are able to extend the extended x-ray absorption fine structure range beyond the onset of the iron absorption edge. This results in improvement in resolution of the manganese-backscatterer distances in PS II from 0.14 to 0.09Ä. The high resolution data obtained from oriented spinach PS II membranes in the S1 state show that there are three di-μ-oxo-bridged manganese-manganese distances of ∼2.7 and ∼2.8Ä in a 2:1 ratio and that these three manganese-manganese vectors are aligned at an average orientation of ∼60° relative to the membrane normal. Furthermore, we are able to observe the separation of the Fourier peaks corresponding to the ∼3.2Ä manganese-manganese and the ∼3.4Ä manganese-calcium interactions in oriented PS II samples and determine their orientation relative to the membrane normal. The average of the manganese-calcium vectors at ∼3.4Ä is aligned along the membrane normal, while the ∼3.2Ä manganese-manganese vector is oriented near the membrane plane. A comparison of this structural information with the proposed Mn4Ca cluster models based on spectroscopic and diffraction data provides input for refining and selecting among these models.
@article{pushkar_structure_2007,
title = {Structure and {Orientation} of the {Mn4Ca} {Cluster} in {Plant} {Photosystem} {II} {Membranes} {Studied} by {Polarized} {Range}-extended {X}-ray {Absorption} {Spectroscopy}*♦},
volume = {282},
issn = {0021-9258},
url = {https://www.sciencedirect.com/science/article/pii/S0021925820635621},
doi = {10.1074/jbc.M610505200},
abstract = {X-ray absorption spectroscopy has provided important insights into the structure and function of the Mn4Ca cluster in the oxygen-evolving complex of Photosystem II (PS II). The range of manganese extended x-ray absorption fine structure data collected from PS II until now has been, however, limited by the presence of iron in PS II. Using a crystal spectrometer with high energy resolution to detect solely the manganese Kα fluorescence, we are able to extend the extended x-ray absorption fine structure range beyond the onset of the iron absorption edge. This results in improvement in resolution of the manganese-backscatterer distances in PS II from 0.14 to 0.09Ä. The high resolution data obtained from oriented spinach PS II membranes in the S1 state show that there are three di-μ-oxo-bridged manganese-manganese distances of ∼2.7 and ∼2.8Ä in a 2:1 ratio and that these three manganese-manganese vectors are aligned at an average orientation of ∼60° relative to the membrane normal. Furthermore, we are able to observe the separation of the Fourier peaks corresponding to the ∼3.2Ä manganese-manganese and the ∼3.4Ä manganese-calcium interactions in oriented PS II samples and determine their orientation relative to the membrane normal. The average of the manganese-calcium vectors at ∼3.4Ä is aligned along the membrane normal, while the ∼3.2Ä manganese-manganese vector is oriented near the membrane plane. A comparison of this structural information with the proposed Mn4Ca cluster models based on spectroscopic and diffraction data provides input for refining and selecting among these models.},
number = {10},
urldate = {2024-11-29},
journal = {Journal of Biological Chemistry},
author = {Pushkar, Yulia and Yano, Junko and Glatzel, Pieter and Messinger, Johannes and Lewis, Azul and Sauer, Kenneth and Bergmann, Uwe and Yachandra, Vittal},
month = mar,
year = {2007},
pages = {7198--7208},
}
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The range of manganese extended x-ray absorption fine structure data collected from PS II until now has been, however, limited by the presence of iron in PS II. Using a crystal spectrometer with high energy resolution to detect solely the manganese Kα fluorescence, we are able to extend the extended x-ray absorption fine structure range beyond the onset of the iron absorption edge. This results in improvement in resolution of the manganese-backscatterer distances in PS II from 0.14 to 0.09Ä. The high resolution data obtained from oriented spinach PS II membranes in the S1 state show that there are three di-μ-oxo-bridged manganese-manganese distances of ∼2.7 and ∼2.8Ä in a 2:1 ratio and that these three manganese-manganese vectors are aligned at an average orientation of ∼60° relative to the membrane normal. Furthermore, we are able to observe the separation of the Fourier peaks corresponding to the ∼3.2Ä manganese-manganese and the ∼3.4Ä manganese-calcium interactions in oriented PS II samples and determine their orientation relative to the membrane normal. The average of the manganese-calcium vectors at ∼3.4Ä is aligned along the membrane normal, while the ∼3.2Ä manganese-manganese vector is oriented near the membrane plane. A comparison of this structural information with the proposed Mn4Ca cluster models based on spectroscopic and diffraction data provides input for refining and selecting among these models.","number":"10","urldate":"2024-11-29","journal":"Journal of Biological Chemistry","author":[{"propositions":[],"lastnames":["Pushkar"],"firstnames":["Yulia"],"suffixes":[]},{"propositions":[],"lastnames":["Yano"],"firstnames":["Junko"],"suffixes":[]},{"propositions":[],"lastnames":["Glatzel"],"firstnames":["Pieter"],"suffixes":[]},{"propositions":[],"lastnames":["Messinger"],"firstnames":["Johannes"],"suffixes":[]},{"propositions":[],"lastnames":["Lewis"],"firstnames":["Azul"],"suffixes":[]},{"propositions":[],"lastnames":["Sauer"],"firstnames":["Kenneth"],"suffixes":[]},{"propositions":[],"lastnames":["Bergmann"],"firstnames":["Uwe"],"suffixes":[]},{"propositions":[],"lastnames":["Yachandra"],"firstnames":["Vittal"],"suffixes":[]}],"month":"March","year":"2007","pages":"7198–7208","bibtex":"@article{pushkar_structure_2007,\n\ttitle = {Structure and {Orientation} of the {Mn4Ca} {Cluster} in {Plant} {Photosystem} {II} {Membranes} {Studied} by {Polarized} {Range}-extended {X}-ray {Absorption} {Spectroscopy}*♦},\n\tvolume = {282},\n\tissn = {0021-9258},\n\turl = {https://www.sciencedirect.com/science/article/pii/S0021925820635621},\n\tdoi = {10.1074/jbc.M610505200},\n\tabstract = {X-ray absorption spectroscopy has provided important insights into the structure and function of the Mn4Ca cluster in the oxygen-evolving complex of Photosystem II (PS II). The range of manganese extended x-ray absorption fine structure data collected from PS II until now has been, however, limited by the presence of iron in PS II. Using a crystal spectrometer with high energy resolution to detect solely the manganese Kα fluorescence, we are able to extend the extended x-ray absorption fine structure range beyond the onset of the iron absorption edge. This results in improvement in resolution of the manganese-backscatterer distances in PS II from 0.14 to 0.09Ä. The high resolution data obtained from oriented spinach PS II membranes in the S1 state show that there are three di-μ-oxo-bridged manganese-manganese distances of ∼2.7 and ∼2.8Ä in a 2:1 ratio and that these three manganese-manganese vectors are aligned at an average orientation of ∼60° relative to the membrane normal. Furthermore, we are able to observe the separation of the Fourier peaks corresponding to the ∼3.2Ä manganese-manganese and the ∼3.4Ä manganese-calcium interactions in oriented PS II samples and determine their orientation relative to the membrane normal. The average of the manganese-calcium vectors at ∼3.4Ä is aligned along the membrane normal, while the ∼3.2Ä manganese-manganese vector is oriented near the membrane plane. A comparison of this structural information with the proposed Mn4Ca cluster models based on spectroscopic and diffraction data provides input for refining and selecting among these models.},\n\tnumber = {10},\n\turldate = {2024-11-29},\n\tjournal = {Journal of Biological Chemistry},\n\tauthor = {Pushkar, Yulia and Yano, Junko and Glatzel, Pieter and Messinger, Johannes and Lewis, Azul and Sauer, Kenneth and Bergmann, Uwe and Yachandra, Vittal},\n\tmonth = mar,\n\tyear = {2007},\n\tpages = {7198--7208},\n}\n\n\n\n","author_short":["Pushkar, Y.","Yano, J.","Glatzel, P.","Messinger, J.","Lewis, A.","Sauer, K.","Bergmann, U.","Yachandra, V."],"key":"pushkar_structure_2007","id":"pushkar_structure_2007","bibbaseid":"pushkar-yano-glatzel-messinger-lewis-sauer-bergmann-yachandra-structureandorientationofthemn4caclusterinplantphotosystemiimembranesstudiedbypolarizedrangeextendedxrayabsorptionspectroscopy-2007","role":"author","urls":{"Paper":"https://www.sciencedirect.com/science/article/pii/S0021925820635621"},"metadata":{"authorlinks":{}},"html":""},"bibtype":"article","biburl":"https://bibbase.org/zotero/upscpub","dataSources":["9cGcv2t8pRzC92kzs"],"keywords":[],"search_terms":["structure","orientation","mn4ca","cluster","plant","photosystem","membranes","studied","polarized","range","extended","ray","absorption","spectroscopy","pushkar","yano","glatzel","messinger","lewis","sauer","bergmann","yachandra"],"title":"Structure and Orientation of the Mn4Ca Cluster in Plant Photosystem II Membranes Studied by Polarized Range-extended X-ray Absorption Spectroscopy*♦","year":2007}