@article{shutova_structural_2005,
	title = {Structural {Dynamics} of the {Manganese}-{Stabilizing} {ProteinEffect} of {pH}, {Calcium}, and {Manganese}},
	volume = {44},
	issn = {0006-2960},
	url = {https://doi.org/10.1021/bi0512750},
	doi = {10.1021/bi0512750},
	abstract = {The photosystem-II-associated 33-kDa extrinsic manganese-stabilizing protein is found in all oxygen-evolving organisms. In this paper, we show that this protein undergoes pH-induced conformational changes in the physiological pH range. At a neutral pH of 7.2, the hydrophobic amino acid residues that are most likely located inside the β barrel are “closed” and the protein binds neither Mn2+ nor Ca2+ ions. When the protein is transferred to a solution with a slightly acidic pH of 5.7, hydrophobic amino acid residues become exposed to the surrounding medium, enabling them to bind the fluorescent probe 8,1-ANS. At this pH-induced open state, Mn2+ and Ca2+ bind to the manganese-stabilizing protein. The pH values used in this study, 7.2 and 5.7, are typical of the pH found in the thylakoid lumen in the dark and light, respectively. A model is presented in which the manganese-stabilizing protein undergoes a pH-dependent conformational change that in turn influences its capacity to bind calcium and manganese. In this model, the proton-dependent conformational changes of the tertiary structure of the manganese-stabilizing protein are of functional relevance for the regulation of substrate (water) delivery to and product (proton) release from the water-oxidizing complex by forming a proton-sensing proton-transport pathway.},
	number = {46},
	urldate = {2021-06-11},
	journal = {Biochemistry},
	author = {Shutova, Tatiana and Nikitina, Julia and Deikus, Gintaras and Andersson, Bertil and Klimov, Vyacheslav and Samuelsson, Göran},
	month = nov,
	year = {2005},
	note = {Publisher: American Chemical Society},
	pages = {15182--15192},
}

{"_id":"x9zGpyNcBHLq3hEEb","bibbaseid":"shutova-nikitina-deikus-andersson-klimov-samuelsson-structuraldynamicsofthemanganesestabilizingproteineffectofphcalciumandmanganese-2005","author_short":["Shutova, T.","Nikitina, J.","Deikus, G.","Andersson, B.","Klimov, V.","Samuelsson, G."],"bibdata":{"bibtype":"article","type":"article","title":"Structural Dynamics of the Manganese-Stabilizing ProteinEffect of pH, Calcium, and Manganese","volume":"44","issn":"0006-2960","url":"https://doi.org/10.1021/bi0512750","doi":"10.1021/bi0512750","abstract":"The photosystem-II-associated 33-kDa extrinsic manganese-stabilizing protein is found in all oxygen-evolving organisms. In this paper, we show that this protein undergoes pH-induced conformational changes in the physiological pH range. At a neutral pH of 7.2, the hydrophobic amino acid residues that are most likely located inside the β barrel are “closed” and the protein binds neither Mn2+ nor Ca2+ ions. When the protein is transferred to a solution with a slightly acidic pH of 5.7, hydrophobic amino acid residues become exposed to the surrounding medium, enabling them to bind the fluorescent probe 8,1-ANS. At this pH-induced open state, Mn2+ and Ca2+ bind to the manganese-stabilizing protein. The pH values used in this study, 7.2 and 5.7, are typical of the pH found in the thylakoid lumen in the dark and light, respectively. A model is presented in which the manganese-stabilizing protein undergoes a pH-dependent conformational change that in turn influences its capacity to bind calcium and manganese. In this model, the proton-dependent conformational changes of the tertiary structure of the manganese-stabilizing protein are of functional relevance for the regulation of substrate (water) delivery to and product (proton) release from the water-oxidizing complex by forming a proton-sensing proton-transport pathway.","number":"46","urldate":"2021-06-11","journal":"Biochemistry","author":[{"propositions":[],"lastnames":["Shutova"],"firstnames":["Tatiana"],"suffixes":[]},{"propositions":[],"lastnames":["Nikitina"],"firstnames":["Julia"],"suffixes":[]},{"propositions":[],"lastnames":["Deikus"],"firstnames":["Gintaras"],"suffixes":[]},{"propositions":[],"lastnames":["Andersson"],"firstnames":["Bertil"],"suffixes":[]},{"propositions":[],"lastnames":["Klimov"],"firstnames":["Vyacheslav"],"suffixes":[]},{"propositions":[],"lastnames":["Samuelsson"],"firstnames":["Göran"],"suffixes":[]}],"month":"November","year":"2005","note":"Publisher: American Chemical Society","pages":"15182–15192","bibtex":"@article{shutova_structural_2005,\n\ttitle = {Structural {Dynamics} of the {Manganese}-{Stabilizing} {ProteinEffect} of {pH}, {Calcium}, and {Manganese}},\n\tvolume = {44},\n\tissn = {0006-2960},\n\turl = {https://doi.org/10.1021/bi0512750},\n\tdoi = {10.1021/bi0512750},\n\tabstract = {The photosystem-II-associated 33-kDa extrinsic manganese-stabilizing protein is found in all oxygen-evolving organisms. In this paper, we show that this protein undergoes pH-induced conformational changes in the physiological pH range. At a neutral pH of 7.2, the hydrophobic amino acid residues that are most likely located inside the β barrel are “closed” and the protein binds neither Mn2+ nor Ca2+ ions. When the protein is transferred to a solution with a slightly acidic pH of 5.7, hydrophobic amino acid residues become exposed to the surrounding medium, enabling them to bind the fluorescent probe 8,1-ANS. At this pH-induced open state, Mn2+ and Ca2+ bind to the manganese-stabilizing protein. The pH values used in this study, 7.2 and 5.7, are typical of the pH found in the thylakoid lumen in the dark and light, respectively. A model is presented in which the manganese-stabilizing protein undergoes a pH-dependent conformational change that in turn influences its capacity to bind calcium and manganese. In this model, the proton-dependent conformational changes of the tertiary structure of the manganese-stabilizing protein are of functional relevance for the regulation of substrate (water) delivery to and product (proton) release from the water-oxidizing complex by forming a proton-sensing proton-transport pathway.},\n\tnumber = {46},\n\turldate = {2021-06-11},\n\tjournal = {Biochemistry},\n\tauthor = {Shutova, Tatiana and Nikitina, Julia and Deikus, Gintaras and Andersson, Bertil and Klimov, Vyacheslav and Samuelsson, Göran},\n\tmonth = nov,\n\tyear = {2005},\n\tnote = {Publisher: American Chemical Society},\n\tpages = {15182--15192},\n}\n\n","author_short":["Shutova, T.","Nikitina, J.","Deikus, G.","Andersson, B.","Klimov, V.","Samuelsson, G."],"key":"shutova_structural_2005","id":"shutova_structural_2005","bibbaseid":"shutova-nikitina-deikus-andersson-klimov-samuelsson-structuraldynamicsofthemanganesestabilizingproteineffectofphcalciumandmanganese-2005","role":"author","urls":{"Paper":"https://doi.org/10.1021/bi0512750"},"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://bibbase.org/zotero/upscpub","dataSources":["9cGcv2t8pRzC92kzs","fvfkWcShg3Mybjoog","Tu3jPdZyJF3j547xT"],"keywords":[],"search_terms":["structural","dynamics","manganese","stabilizing","proteineffect","calcium","manganese","shutova","nikitina","deikus","andersson","klimov","samuelsson"],"title":"Structural Dynamics of the Manganese-Stabilizing ProteinEffect of pH, Calcium, and Manganese","year":2005}