| 1. |
- Eskling, Marie, et al.
(författare)
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Changes in the quantities of violaxanthin de-epoxidase, xanthophylls and ascorbate in spinach upon shift from low to high light
- 1998
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Ingår i: Photosynthesis Research. - 0166-8595. ; 57:1, s. 41-50
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Tidskriftsartikel (refereegranskat)abstract
- Zeaxanthin, a carotenoid in the xanthophyll cycle, has been suggested to play a role in the protection against photodestruction. We have studied the importance of the parameters involved in zeaxanthin formation by comparing spinach plants grown in low light (100 to 250 mol m-2 s-1) to plants transferred to high light (950 mol m-2 s-1). Different parameters were followed for a total of 11 days. Our experiments show that violaxanthin de-epoxidase decreased between 15 and 30%, the quantity of xanthophyll cycle pigments doubled to 100 mmol (mol Chl)-1, corresponding to 27 mol m-2, and the rate of violaxanthin to zeaxanthin conversion was doubled. Lutein and neoxanthin increased from 50 to 71 mol m-2 and from 16 to 23 mol m-2, respectively. On a leaf area basis, chlorophyll and -carotene levels first decreased and then after 4 days increased. The chlorophyll a/b ratio was unchanged. The quantity of ascorbate was doubled to 2 mmol m-2, corresponding to an estimated increase in the chloroplasts from 25 to 50 mM. In view of our data, we propose that the increase in xanthophyll cycle pigments and ascorbate only partly explain the increased rate of conversion of violaxanthin to zeaxanthin, but the most probable explanation of the faster conversion is an increased accessibility of violaxanthin in the membrane.
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| 2. |
- Geijer, Paulina, et al.
(författare)
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Simultaneous detection of spin-coupled and decoupled QA- EPR-signals in Photosystem II complexes isolated with isoelectric focusing
- 1998
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Ingår i: Photosynthesis Research. - 0166-8595. ; 58:3, s. 231-243
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Tidskriftsartikel (refereegranskat)abstract
- The Photosystem II multisubunit protein complex can be extracted from thylakoid membranes with non-ionic detergents and subjected to various spectroscopical and biochemical investigations. This paper shows that after extraction with dodecyl-beta-D-maltoside, several Photosystem II complexes could be resolved by isoelectric focusing. Structurally, the various Photosystem II complexes differed from each other in polypeptide composition, especially with regard to the chlorophyll a/b-binding proteins, which gave rise to differing isoelectric points. Functionally, the various Photosystem II complexes differed from each other on the acceptor side, as judged by acceptor side-dependent electron transfer and electron paramagnetic resonance (EPR). The Q_{A}^- Fe2+-signal (g = 1.84), arising from Q_{A}^- spin-coupled to the acceptor-side iron, and a radical signal arising from decoupled Q_{A}^- (g = 2.0045) could be detected simultaneously in some of the Photosystem II complexes, and the amount of each of the two signals were inversely related. The results are discussed in relation to previously known heterogeneities in Photosystem II.
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