@article{shutova_comparative_2003,
	title = {Comparative studies on the properties of the extrinsic manganese-stabilizing protein from higher plants and of a synthetic peptide of its {C}-terminus},
	volume = {1604},
	issn = {0005-2728},
	doi = {10/cx7k4m},
	abstract = {The present study describes a comparative analysis on the fluorescence properties of the manganese-stabilizing protein (MSP), a synthetic peptide corresponding to its C terminus and a 7:1 (molar ratio) mixture of N-acetyl-tyrosine and N-acetyl-tryptophan, respectively, together with reconstitution experiments of oxygen evolution in MSP-depleted photosystem II (PS II) membrane fragments. It is found: (i) at neutral pH, the fluorescence from Trp(241) is strongly diminished in MSP solutions, whereas it highly dominates the overall emission from the C-terminus peptide; (ii) at alkaline pH, the emission of Tyr and Trp is quenched in both, MSP and C-terminus peptide, with increasing pH but the decline curve is shifted by about two pH units towards the alkaline region in MSP; (iii) a drastically different pattern emerges in the 7:1 mixture where the Trp emission even slightly increases at high pH; (iv) the anisotropy of the fluorescence emission is wavelength-independent (310-395 nm) and indicative of one emitter type (Trp) in the C-terminus peptide and of two emitter types (Tyr, Trp) in MSP; and (v) in MSP-depleted PS H membrane fragments the oxygen evolution is restored (up to 85\% of untreated control) by rebinding of MSP but not by the C-terminus peptide, however, the presence of the latter diminishes the restoration effect of MSP. A quenching mechanism of Trp fluorescence by a next neighbored tyrosinate in the peptide chain is proposed and the relevance of the C terminus of MSP briefly discussed. (C) 2003 Elsevier Science B.V. All rights reserved.},
	language = {English},
	number = {2},
	journal = {Biochimica Et Biophysica Acta-Bioenergetics},
	author = {Shutova, T. and Villarejo, A. and Zietz, B. and Klimov, V. and Gillbro, T. and Samuelsson, G. and Renger, G.},
	month = jun,
	year = {2003},
	note = {Place: Amsterdam
Publisher: Elsevier Science Bv
WOS:000183222900005},
	keywords = {33 kda, 33-kda protein, C-terminus synthetic peptide, chlamydomonas-reinhardtii, molten globule, msp, oxygen-evolving complex, photosystem II, proton-transfer, ps-ii, reconstitution of   oxygen evolution, spinach photosystem-ii, synechococcus-elongatus, tryptophan fluorescence, tyrosine and tryptophan fluorescence},
	pages = {95--104},
}

{"_id":"W69tWBvTumtKLTwvH","bibbaseid":"shutova-villarejo-zietz-klimov-gillbro-samuelsson-renger-comparativestudiesonthepropertiesoftheextrinsicmanganesestabilizingproteinfromhigherplantsandofasyntheticpeptideofitscterminus-2003","author_short":["Shutova, T.","Villarejo, A.","Zietz, B.","Klimov, V.","Gillbro, T.","Samuelsson, G.","Renger, G."],"bibdata":{"bibtype":"article","type":"article","title":"Comparative studies on the properties of the extrinsic manganese-stabilizing protein from higher plants and of a synthetic peptide of its C-terminus","volume":"1604","issn":"0005-2728","doi":"10/cx7k4m","abstract":"The present study describes a comparative analysis on the fluorescence properties of the manganese-stabilizing protein (MSP), a synthetic peptide corresponding to its C terminus and a 7:1 (molar ratio) mixture of N-acetyl-tyrosine and N-acetyl-tryptophan, respectively, together with reconstitution experiments of oxygen evolution in MSP-depleted photosystem II (PS II) membrane fragments. It is found: (i) at neutral pH, the fluorescence from Trp(241) is strongly diminished in MSP solutions, whereas it highly dominates the overall emission from the C-terminus peptide; (ii) at alkaline pH, the emission of Tyr and Trp is quenched in both, MSP and C-terminus peptide, with increasing pH but the decline curve is shifted by about two pH units towards the alkaline region in MSP; (iii) a drastically different pattern emerges in the 7:1 mixture where the Trp emission even slightly increases at high pH; (iv) the anisotropy of the fluorescence emission is wavelength-independent (310-395 nm) and indicative of one emitter type (Trp) in the C-terminus peptide and of two emitter types (Tyr, Trp) in MSP; and (v) in MSP-depleted PS H membrane fragments the oxygen evolution is restored (up to 85% of untreated control) by rebinding of MSP but not by the C-terminus peptide, however, the presence of the latter diminishes the restoration effect of MSP. A quenching mechanism of Trp fluorescence by a next neighbored tyrosinate in the peptide chain is proposed and the relevance of the C terminus of MSP briefly discussed. (C) 2003 Elsevier Science B.V. All rights reserved.","language":"English","number":"2","journal":"Biochimica Et Biophysica Acta-Bioenergetics","author":[{"propositions":[],"lastnames":["Shutova"],"firstnames":["T."],"suffixes":[]},{"propositions":[],"lastnames":["Villarejo"],"firstnames":["A."],"suffixes":[]},{"propositions":[],"lastnames":["Zietz"],"firstnames":["B."],"suffixes":[]},{"propositions":[],"lastnames":["Klimov"],"firstnames":["V."],"suffixes":[]},{"propositions":[],"lastnames":["Gillbro"],"firstnames":["T."],"suffixes":[]},{"propositions":[],"lastnames":["Samuelsson"],"firstnames":["G."],"suffixes":[]},{"propositions":[],"lastnames":["Renger"],"firstnames":["G."],"suffixes":[]}],"month":"June","year":"2003","note":"Place: Amsterdam Publisher: Elsevier Science Bv WOS:000183222900005","keywords":"33 kda, 33-kda protein, C-terminus synthetic peptide, chlamydomonas-reinhardtii, molten globule, msp, oxygen-evolving complex, photosystem II, proton-transfer, ps-ii, reconstitution of oxygen evolution, spinach photosystem-ii, synechococcus-elongatus, tryptophan fluorescence, tyrosine and tryptophan fluorescence","pages":"95–104","bibtex":"@article{shutova_comparative_2003,\n\ttitle = {Comparative studies on the properties of the extrinsic manganese-stabilizing protein from higher plants and of a synthetic peptide of its {C}-terminus},\n\tvolume = {1604},\n\tissn = {0005-2728},\n\tdoi = {10/cx7k4m},\n\tabstract = {The present study describes a comparative analysis on the fluorescence properties of the manganese-stabilizing protein (MSP), a synthetic peptide corresponding to its C terminus and a 7:1 (molar ratio) mixture of N-acetyl-tyrosine and N-acetyl-tryptophan, respectively, together with reconstitution experiments of oxygen evolution in MSP-depleted photosystem II (PS II) membrane fragments. It is found: (i) at neutral pH, the fluorescence from Trp(241) is strongly diminished in MSP solutions, whereas it highly dominates the overall emission from the C-terminus peptide; (ii) at alkaline pH, the emission of Tyr and Trp is quenched in both, MSP and C-terminus peptide, with increasing pH but the decline curve is shifted by about two pH units towards the alkaline region in MSP; (iii) a drastically different pattern emerges in the 7:1 mixture where the Trp emission even slightly increases at high pH; (iv) the anisotropy of the fluorescence emission is wavelength-independent (310-395 nm) and indicative of one emitter type (Trp) in the C-terminus peptide and of two emitter types (Tyr, Trp) in MSP; and (v) in MSP-depleted PS H membrane fragments the oxygen evolution is restored (up to 85\\% of untreated control) by rebinding of MSP but not by the C-terminus peptide, however, the presence of the latter diminishes the restoration effect of MSP. A quenching mechanism of Trp fluorescence by a next neighbored tyrosinate in the peptide chain is proposed and the relevance of the C terminus of MSP briefly discussed. (C) 2003 Elsevier Science B.V. All rights reserved.},\n\tlanguage = {English},\n\tnumber = {2},\n\tjournal = {Biochimica Et Biophysica Acta-Bioenergetics},\n\tauthor = {Shutova, T. and Villarejo, A. and Zietz, B. and Klimov, V. and Gillbro, T. and Samuelsson, G. and Renger, G.},\n\tmonth = jun,\n\tyear = {2003},\n\tnote = {Place: Amsterdam\nPublisher: Elsevier Science Bv\nWOS:000183222900005},\n\tkeywords = {33 kda, 33-kda protein, C-terminus synthetic peptide, chlamydomonas-reinhardtii, molten globule, msp, oxygen-evolving complex, photosystem II, proton-transfer, ps-ii, reconstitution of oxygen evolution, spinach photosystem-ii, synechococcus-elongatus, tryptophan fluorescence, tyrosine and tryptophan fluorescence},\n\tpages = {95--104},\n}\n\n\n\n","author_short":["Shutova, T.","Villarejo, A.","Zietz, B.","Klimov, V.","Gillbro, T.","Samuelsson, G.","Renger, G."],"key":"shutova_comparative_2003","id":"shutova_comparative_2003","bibbaseid":"shutova-villarejo-zietz-klimov-gillbro-samuelsson-renger-comparativestudiesonthepropertiesoftheextrinsicmanganesestabilizingproteinfromhigherplantsandofasyntheticpeptideofitscterminus-2003","role":"author","urls":{},"keyword":["33 kda","33-kda protein","C-terminus synthetic peptide","chlamydomonas-reinhardtii","molten globule","msp","oxygen-evolving complex","photosystem II","proton-transfer","ps-ii","reconstitution of oxygen evolution","spinach photosystem-ii","synechococcus-elongatus","tryptophan fluorescence","tyrosine and tryptophan fluorescence"],"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://bibbase.org/zotero/upscpub","dataSources":["9cGcv2t8pRzC92kzs","fvfkWcShg3Mybjoog","Tu3jPdZyJF3j547xT","3zTPPmKj8BiTcpc6C"],"keywords":["33 kda","33-kda protein","c-terminus synthetic peptide","chlamydomonas-reinhardtii","molten globule","msp","oxygen-evolving complex","photosystem ii","proton-transfer","ps-ii","reconstitution of oxygen evolution","spinach photosystem-ii","synechococcus-elongatus","tryptophan fluorescence","tyrosine and tryptophan fluorescence"],"search_terms":["comparative","studies","properties","extrinsic","manganese","stabilizing","protein","higher","plants","synthetic","peptide","terminus","shutova","villarejo","zietz","klimov","gillbro","samuelsson","renger"],"title":"Comparative studies on the properties of the extrinsic manganese-stabilizing protein from higher plants and of a synthetic peptide of its C-terminus","year":2003}