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Spermine is a potent modulator of proton transport through LHCII created by Theodoros Tsiavos, Nikolaos E. Ioannidis, Achilleas Tsortos, Electra Gizeli and Kiriakos Kotzabasis

By: Contributor(s): Material type: TextTextSeries: Journal of Plant Physiology ; Volume 177Amsterdam: Elsevier GmbH, 2015Content type:
  • text
Media type:
  • unmediated
Carrier type:
  • volume
ISSN:
  • 0176-1617
Subject(s): LOC classification:
  • QK711.2 JOU
Online resources: Abstract: 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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Item type Current library Call number Vol info Status Notes Date due Barcode
Journal Article Journal Article Main Library Journal Article QK711.2 JOU (Browse shelf(Opens below)) Vol.177 (pages44-50) Not for loan For in house use only
Journal Article Journal Article 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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