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Obscurity of chlorophyll tails - Is chlorophyll with farnesyl tail incorporated into PSII complexes?

Authors :
Graça AT
Lihavainen J
Hussein R
Schröder WP
Source :
Physiologia plantarum [Physiol Plant] 2024 Jul-Aug; Vol. 176 (4), pp. e14428.
Publication Year :
2024

Abstract

Chlorophyll is essential in photosynthesis, converting sunlight into chemical energy in plants, algae, and certain bacteria. Its structure, featuring a porphyrin ring enclosing a central magnesium ion, varies in forms like chlorophyll a, b, c, d, and f, allowing light absorption at a broader spectrum. With a 20-carbon phytyl tail (except for chlorophyll c), chlorophyll is anchored to proteins. Previous findings suggested the presence of chlorophyll with a modified farnesyl tail in thermophilic cyanobacteria Thermosynechoccocus vestitus. In our Arabidopsis thaliana PSII cryo-EM map, specific chlorophylls showed incomplete phytyl tails, suggesting potential farnesyl modifications. However, further high-resolution mass spectrometry (HRMS) analysis in A. thaliana and T. vestitus did not confirm the presence of any farnesyl tails. Instead, we propose the truncated tails in PSII models may result from binding pocket flexibility rather than actual modifications.<br /> (© 2024 The Author(s). Physiologia Plantarum published by John Wiley & Sons Ltd on behalf of Scandinavian Plant Physiology Society.)

Details

Language :
English
ISSN :
1399-3054
Volume :
176
Issue :
4
Database :
MEDLINE
Journal :
Physiologia plantarum
Publication Type :
Academic Journal
Accession number :
38981693
Full Text :
https://doi.org/10.1111/ppl.14428