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| 003 | ZW-GwMSU | ||
| 005 | 20250314081433.0 | ||
| 008 | 250314b |||||||| |||| 00| 0 eng d | ||
| 022 | _a0176-1617 | ||
| 040 |
_aMSU _bEnglish _cMSU _erda |
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| 050 | 0 | 0 | _aQK711.2 JOU |
| 100 | 1 |
_aTsiavos, Theodoros _eauthor |
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| 245 | 1 | 0 |
_aSpermine is a potent modulator of proton transport through LHCII _ccreated by Theodoros Tsiavos, Nikolaos E. Ioannidis, Achilleas Tsortos, Electra Gizeli and Kiriakos Kotzabasis |
| 264 | 1 |
_aAmsterdam: _bElsevier GmbH, _c2015. |
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| 336 |
_2rdacontent _atext _btxt |
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| 337 |
_2rdamedia _aunmediated _bn |
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| 338 |
_2rdacarrier _avolume _bnc |
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| 440 |
_aJournal of Plant Physiology _vVolume 177 |
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| 520 | 3 | _aThe effect of spermine on proton transport across large unilamellar liposomes containing incorporated complexes of the PSII antenna has been studied with the application of a pH-sensitive dye entrapped inside the vesicles. Both monomeric LHCbs and trimeric LHCII increased the permeability of proteoliposomes to protons when in a partly aggregated state within the lipid membrane. We have previously shown that a spermine-induced conformational change in LHCII results in its aggregation and ultimately in the enhancement of excitation energy as heat (qE). In this paper, spermine-induced aggregation of LHCII was found to facilitate proton transport across the proteoliposomes, indicating that a second protective mechanism (other than qE) might exist and might be regulated in vivo by polyamines when photosynthesis is saturated in excess light. | |
| 650 | _aAggregation | ||
| 650 | _aLight harvesting complex II | ||
| 650 | _aLiposomes | ||
| 700 | 1 |
_aIoannidis, Nikolaos E. _eco-author |
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| 700 | 1 |
_aTsortos, Achilleas _eco-author |
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| 700 | 1 |
_aGizeli, Electra _eco-author |
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| 700 | 1 |
_aKotzabasis, Kiriakos _eco-author |
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| 856 | _uhttps://doi.org/10.1016/j.jplph.2015.01.010 | ||
| 942 |
_2lcc _cJA |
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| 999 |
_c169285 _d169285 |
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