Photoprotection of Photosynthetic Pigments in Plant One-Helix Protein 1/2 Heterodimers
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články
- MeSH
- Arabidopsis chemie MeSH
- chlorofyl chemie MeSH
- fotochemické procesy MeSH
- fotosyntéza MeSH
- karotenoidy chemie MeSH
- kinetika MeSH
- konformace proteinů MeSH
- kyslík chemie MeSH
- multimerizace proteinu MeSH
- přenos energie MeSH
- proteiny huseníčku chemie MeSH
- proteiny vázající chlorofyl chemie MeSH
- světlosběrné proteinové komplexy chemie MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- chlorofyl MeSH
- karotenoidy MeSH
- kyslík MeSH
- OHP1 protein, Arabidopsis MeSH Prohlížeč
- Ohp2 protein, Arabidopsis MeSH Prohlížeč
- proteiny huseníčku MeSH
- proteiny vázající chlorofyl MeSH
- světlosběrné proteinové komplexy MeSH
One-helix proteins 1 and 2 (OHP1/2) are members of the family of light-harvesting-like proteins (LIL) in plants, and their potential function(s) have been initially analyzed only recently. OHP1 and OHP2 are structurally related to the transmembrane α-helices 1 and 3 of all members of the light-harvesting complex (LHC) superfamily. Arabidopsis thaliana OHPs form heterodimers which bind 6 chlorophylls (Chls) a and two carotenoids in vitro. Their function remains unclear, and therefore, a spectroscopic study with reconstituted OHP1/OHP2-complexes was performed. Steady-state spectroscopy did not indicate singlet excitation energy transfer between pigments. Thus, a light-harvesting function can be excluded. Possible pigment-storage and/or -delivery functions of OHPs require photoprotection of the bound Chls. Hence, Chl and carotenoid triplet formation and decays in reconstituted OHP1/2 dimers were measured using nanosecond transient absorption spectroscopy. Unlike in all other photosynthetic LHCs, unquenched Chl triplets were observed with unusually long lifetimes. Moreover, there were virtually no differences in both Chl and carotenoid triplet state lifetimes under either aerobic or anaerobic conditions. The results indicate that both Chls and carotenoids are shielded by the proteins from interactions with ambient oxygen and, thus, protected against formation of singlet oxygen. Only a minor portion of the Chl triplets was quenched by carotenoids. These results are in stark contrast to all previously observed photoprotective processes in LHC/LIL proteins and, thus, may constitute a novel mechanism of photoprotection in the plant photosynthetic apparatus.
Citace poskytuje Crossref.org
Photosynthetic Light-Harvesting (Antenna) Complexes-Structures and Functions