The neoxanthin binding site of the major light harvesting complex (LHCII) from higher plants

Croce, Roberta; Remelli, Rosaria; Varotto, Claudio; Breton, Jacques; Bassi, Roberto

doi:10.1016/s0014-5793(99)00907-2

Cited by 117 publications

(121 citation statements)

References 24 publications

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“…Thus, pigment binding of at least one carotenoidbinding site of each LHCI protein seems to be flexible, allowing occupation by different carotenoids depending on their presence during reconstitution. Such flexibility of some carotenoidbinding sites has already been described for minor LHCIIs and LHCIIb (37)(38)(39)(40).…”

Section: Lhca5 a Novel Light-harvesting Proteinmentioning

confidence: 52%

Pigment Binding, Fluorescence Properties, and Oligomerization Behavior of Lhca5, a Novel Light-harvesting Protein

Storf

Jansson

Schmid

2005

Journal of Biological Chemistry

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Section: Lhca5 a Novel Light-harvesting Proteinmentioning

confidence: 52%

Pigment Binding, Fluorescence Properties, and Oligomerization Behavior of Lhca5, a Novel Light-harvesting Protein

Storf

Jansson

Schmid

2005

Journal of Biological Chemistry

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“…This supports the observation that lutein and zeaxanthin are discriminated against for in N1 because of their structures. Occupancy of N1 is not required for complex reassembly (or subsequent stability (26,27)), but binding of neoxanthin greatly improves the complex yield. Carotenoids with a C-5-C-6 epoxide, but not the C-3-C-6, on at least one end group can occupy N1, as can the diol lactucaxanthin (see below).…”

Section: Discussionmentioning

confidence: 99%

“…This demonstrates that lactucaxanthin can in fact readily bind to at least two xanthophyll binding sites, namely N1 and at least one of the luteinbinding sites. The inability of lactucaxanthin to permit complex assembly suggests that it is omitted from L1, occupancy of which is obligatory for protein folding (26,27), and instead occupies L2. Binding saturates at approximately two molecules of lutein per molecule of lactucaxanthin for each complex (assuming 12 Chl per LHC), indicating that lactucaxanthin readily occupies N1, whereas lutein is excluded.…”

Section: Discussionmentioning

confidence: 99%

The Binding of Xanthophylls to the Bulk Light-harvesting Complex of Photosystem II of Higher Plants

Phillip¹,

Hobe²,

Paulsen³

et al. 2002

Journal of Biological Chemistry

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The pigment composition of the light-harvesting complexes (LHCs) of higher plants is highly conserved. The bulk complex (LHCIIb) binds three xanthophyll molecules in combination with chlorophyll (Chl) a and b. The structural requirements for binding xanthophylls to LHCIIb have been examined using an in vitro reconstitution procedure. Reassembly of the monomeric recombinant LHCIIb was performed using a wide range of native and nonnative xanthophylls, and a specific requirement for the presence of a hydroxy group at C-3 on a single ␤-end group was identified. The presence of additional substituents (e.g. at C-4) did not interfere with xanthophyll binding, but they could not, on their own, support reassembly. cis isomers of zeaxanthin, violaxanthin, and lutein were not bound, whereas all-transneoxanthin and different chiral forms of lutein and zeaxanthin were incorporated into the complex. The C-3 and C-3 diols lactucaxanthin (a carotenoid native to many plant LHCs) and eschscholtzxanthin (a retro-carotenoid) both behaved very differently from lutein and zeaxanthin in that they would not support complex reassembly when used alone. Lactucaxanthin could, however, be bound when lutein was also present, and it showed a high affinity for xanthophyll binding site N1. In the presence of lutein, lactucaxanthin was readily bound to at least one lutein-binding site, suggesting that the ability to bind to the complex and initiate protein folding may be dependent on different structural features of the carotenoid molecule. The importance of carotenoid end group structure and ring-to-chain conformation around the C-6 -C-7 torsion angle of the carotenoid molecule in binding and complex reassembly is discussed.

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“…We suggest that (53). Abbreviations: Lut1 and Lut2, the positions of lutein 1 and lutein 2; Neo, the proposed position of the neoxanthin binding site as inferred from spectroscopic measurements (54). (C) Proposed domain structure of LHCII.…”

Section: Pigment Composition Of Monomeric Lhciimentioning

confidence: 99%

The Functional Significance of the Monomeric and Trimeric States of the Photosystem II Light Harvesting Complexes

2003

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The main light harvesting complex of photosystem II in plants, LHCII, exists in a trimeric state. To understand the biological significance of trimerization, a comparison has been made been LHCII trimers and LHCII monomers prepared by treatment with phospholipase. The treatment used caused no loss of chlorophyll, but there was a difference in carotenoid composition, together with the previously observed alterations in absorption spectrum. It was found that, when compared to monomers, LHCII trimers showed increased thermal stability and a reduced structural flexibility as determined by the decreased rate and amplitude of fluorescence quenching in low-detergent concentration. It is suggested that LHCII should be considered as having two interacting domains: the lutein 1 domain, the site of fluorescence quenching [Wentworth et al. (2003) J. Biol. Chem. 278, 21845-21850], and the lutein 2 domain. The lutein 2 domain faces the interior of the trimer, the differences in absorption spectrum and carotenoid binding in trimers compared to monomers indicating that the trimeric state modulates the conformation of this domain. It is suggested that the lutein 2 domain controls the conformation of the lutein 1 domain, thereby providing allosteric control of fluorescence quenching in LHCII. Thus, the pigment configuration and protein conformation in trimers is adapted for efficient light harvesting and enhanced protein stability. Furthermore, trimers exhibit the optimum level of control of energy dissipation by modulating the development of the quenched state of the complex.

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The neoxanthin binding site of the major light harvesting complex (LHCII) from higher plants

Cited by 117 publications

References 24 publications

Pigment Binding, Fluorescence Properties, and Oligomerization Behavior of Lhca5, a Novel Light-harvesting Protein

Pigment Binding, Fluorescence Properties, and Oligomerization Behavior of Lhca5, a Novel Light-harvesting Protein

The Binding of Xanthophylls to the Bulk Light-harvesting Complex of Photosystem II of Higher Plants

The Functional Significance of the Monomeric and Trimeric States of the Photosystem II Light Harvesting Complexes

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