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Carotenoids Do Not Protect Bacteriochlorophylls in Isolated Light-Harvesting LH2 Complexes of Photosynthetic Bacteria from Destructive Interactions with Singlet Oxygen.

ABSTRACT: The effect of singlet oxygen on light-harvesting (LH) complexes has been studied for a number of sulfur (S⁺) and nonsulfur (S^-) photosynthetic bacteria. The visible/near-IR absorption spectra of the standard LH2 complexes (B800-850) of Allochromatium (Alc.) vinosum (S⁺), Rhodobacter (Rba.) sphaeroides (S^-), Rhodoblastus (Rbl.) acidophilus (S^-), and Rhodopseudomonas (Rps.) palustris (S^-), two types LH2/LH3 (B800-850 and B800-830) of Thiorhodospira (T.) sibirica (S⁺), and an unusual LH2 complex (B800-827) of Marichromatium (Mch.) purpuratum (S⁺) or the LH1 complex from Rhodospirillum (Rsp.) rubrum (S^-) were measured in aqueous buffer suspensions in the presence of singlet oxygen generated by the illumination of the dye Rose Bengal (RB). The content of carotenoids in the samples was determined using HPLC analysis. The LH2 complex of Alc. vinosum and T. sibirica with a reduced content of carotenoids was obtained from cells grown in the presence of diphenylamine (DPA), and LH complexes were obtained from the carotenoidless mutant of Rba. sphaeroides R26.1 and Rps. rubrum G9. We found that LH2 complexes containing a complete set of carotenoids were quite resistant to the destructive action of singlet oxygen in the case of Rba. sphaeroides and Mch. purpuratum. Complexes of other bacteria were much less stable, which can be judged by a strong irreversible decrease in the bacteriochlorophyll (BChl) absorption bands (at 850 or 830 nm, respectively) for sulfur bacteria and absorption bands (at 850 and 800 nm) for nonsulfur bacteria. Simultaneously, we observe the appearance of the oxidized product 3-acetyl-chlorophyll (AcChl) absorbing near 700 nm. Moreover, a decrease in the amount of carotenoids enhanced the spectral stability to the action of singlet oxygen of the LH2 and LH3 complexes from sulfur bacteria and kept it at the same level as in the control samples for carotenoidless mutants of nonsulfur bacteria. These results are discussed in terms of the current hypothesis on the protective functions of carotenoids in bacterial photosynthesis. We suggest that the ability of carotenoids to quench singlet oxygen (well-established in vitro) is not well realized in photosynthetic bacteria. We compared the oxidation of BChl850 in LH2 complexes of sulfur bacteria under the action of singlet oxygen (in the presence of 50 μM RB) or blue light absorbed by carotenoids. These processes are very similar: {[BChl + (RB or carotenoid) + light] + O₂} → AcChl. We speculate that carotenoids are capable of generating singlet oxygen when illuminated. The mechanism of this process is not yet clear.

SUBMITTER: Makhneva ZK

PROVIDER: S-EPMC8434301 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:Steady-state and ultrafast time-resolved optical spectroscopic investigations have been carried out at 293 and 10 K on LH2 pigment-protein complexes isolated from three different strains of photosynthetic bacteria: Rhodobacter (Rb.) sphaeroides G1C, Rb. sphaeroides 2.4.1 (anaerobically and aerobically grown), and Rps. acidophila 10050. The LH2 complexes obtained from these strains contain the carotenoids, neurosporene, spheroidene, spheroidenone, and rhodopin glucoside, respectively. These molecules have a systematically increasing number of pi-electron conjugated carbon-carbon double bonds. Steady-state absorption and fluorescence excitation experiments have revealed that the total efficiency of energy transfer from the carotenoids to bacteriochlorophyll is independent of temperature and nearly constant at approximately 90% for the LH2 complexes containing neurosporene, spheroidene, spheroidenone, but drops to approximately 53% for the complex containing rhodopin glucoside. Ultrafast transient absorption spectra in the near-infrared (NIR) region of the purified carotenoids in solution have revealed the energies of the S1 (2(1)Ag-)-->S2 (1(1)Bu+) excited-state transitions which, when subtracted from the energies of the S0 (1(1)Ag-)-->S2 (1(1)Bu+) transitions determined by steady-state absorption measurements, give precise values for the positions of the S1 (2(1)Ag-) states of the carotenoids. Global fitting of the ultrafast spectral and temporal data sets have revealed the dynamics of the pathways of de-excitation of the carotenoid excited states. The pathways include energy transfer to bacteriochlorophyll, population of the so-called S* state of the carotenoids, and formation of carotenoid radical cations (Car*+). The investigation has found that excitation energy transfer to bacteriochlorophyll is partitioned through the S1 (1(1)Ag-), S2 (1(1)Bu+), and S* states of the different carotenoids to varying degrees. This is understood through a consideration of the energies of the states and the spectral profiles of the molecules. A significant finding is that, due to the low S1 (2(1)Ag-) energy of rhodopin glucoside, energy transfer from this state to the bacteriochlorophylls is significantly less probable compared to the other complexes. This work resolves a long-standing question regarding the cause of the precipitous drop in energy transfer efficiency when the extent of pi-electron conjugation of the carotenoid is extended from ten to eleven conjugated carbon-carbon double bonds in LH2 complexes from purple photosynthetic bacteria.

Project description:Chlorophototrophic organisms have a charge-separating reaction centre (RC) complex that receives energy from a dedicated light-harvesting (LH) antenna. In the purple phototrophic bacteria, these two functions are embodied by the 'core' photosynthetic component, the RC-LH1 complex. RC-LH1 complexes sit within a membrane bilayer, with the central RC wholly or partly surrounded by a curved array of LH1 subunits that bind a series of bacteriochlorophyll (BChl) and carotenoid pigments. Decades of research have shown that the absorption of light initiates a cascade of energy, electron, and proton transfers that culminate in the formation of a quinol, which is subsequently oxidized by the cytochrome bc1 complex. However, a full understanding of all these processes, from femtosecond absorption of light to millisecond quinone diffusion, requires a level of molecular detail that was lacking until the remarkable recent upsurge in the availability of RC-LH1 structures. Here, we survey 13 recently determined RC-LH1 assemblies, and we compare the precise molecular arrangements of pigments and proteins that allow efficient light absorption and the transfer of energy, electrons and protons. We highlight shared structural features, as well as differences that span the bound pigments and cofactors, the structures of individual subunits, the overall architecture of the complexes, and the roles of additional subunits newly identified in just one or a few species. We discuss RC-LH1 structures in the context of prior biochemical and spectroscopic investigations, which together enhance our understanding of the molecular mechanisms of photosynthesis in the purple phototrophic bacteria. A particular emphasis is placed on how the remarkable and unexpected structural diversity in RC-LH1 complexes demonstrates different evolutionary solutions for maximising pigment density for optimised light harvesting, whilst balancing the requirement for efficient quinone diffusion between RC and cytochrome bc1 complexes through the encircling LH1 complex.

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Carotenoids Do Not Protect Bacteriochlorophylls in Isolated Light-Harvesting LH2 Complexes of Photosynthetic Bacteria from Destructive Interactions with Singlet Oxygen.

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