Spermine is a potent modulator of proton transport through LHCII created by Theodoros Tsiavos, Nikolaos E. Ioannidis, Achilleas Tsortos, Electra Gizeli and Kiriakos Kotzabasis
Material type:
- text
- unmediated
- volume
- 0176-1617
- QK711.2 JOU
Item type | Current library | Call number | Vol info | Status | Notes | Date due | Barcode | |
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Main Library Journal Article | QK711.2 JOU (Browse shelf(Opens below)) | Vol.177 (pages44-50) | Not for loan | For in house use only | |||
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Main Library Journal Article | QK711.2 JOU (Browse shelf(Opens below)) | Vol.177 (pages44-50) | Not for loan | For in house use only |
The 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.
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