The reaction center-light harvesting 1 (RC-LH1) complex converts solar energy into electrical energy, driving the initiation of photosynthesis. The authors present a cryo-electron microscopy structure of the RC-LH1 isolated from a marine photoheterotrophic bacterium Dinoroseobacter shibae. The RC comprises four subunits, including a three-heme cytochrome (Cyt) c protein, and is surrounded by a closed LH ring composed of 17 pairs of antenna subunits. Notably, a novel subunit with an N-terminal "helix-turn-helix" motif embedded in the gap between the RC and the LH ring is identified. The purified RC-LH1 complex exhibits high stability in solutions containing Mg2+ or Ca2+. The periplasmic Cyt c2 is predicted to bind at the junction between the Cyt subunit and the membrane plane, enabling electron transfer from Cyt c2 to the proximal heme of the tri-heme Cyt, and subsequently to the special pair of bacteriochlorophylls. These findings provide structural insights into the efficient energy and electron transfer processes within a distinct type of RC-LH1, and shed light on evolutionary adaptations of photosynthesis.

• Klíčová slova
• energy transfer, photoheterotrophic bacteria, photosynthesis, reaction center, structure,
• MeSH
• bakteriální proteiny metabolismus   chemie   MeSH
• elektronová kryomikroskopie metody   MeSH
• fotosyntéza fyziologie   MeSH
• hem metabolismus   chemie   MeSH
• světlosběrné proteinové komplexy * metabolismus   ultrastruktura   chemie   MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• bakteriální proteiny MeSH
• hem MeSH
• světlosběrné proteinové komplexy * MeSH

In bacterial photosynthesis, the excitation energy transfer (EET) from carotenoids to bacteriochlorophyll a has a significant impact on the overall efficiency of the primary photosynthetic process. This efficiency can be enhanced when the involved carotenoid has intramolecular charge-transfer (ICT) character, as found in light-harvesting systems of marine alga and diatoms. Here, we provide insights into the significance of ICT excited states following the incorporation of a higher plant carotenoid, β-apo-8'-carotenal, into the carotenoidless light-harvesting 1 (LH1) complex of the purple photosynthetic bacterium Rhodospirillum rubrum strain G9+. β-apo-8'-carotenal generates the ICT excited state in the reconstituted LH1 complex, achieving an efficiency of EET of up to 79%, which exceeds that found in the wild-type LH1 complex.

• Publikační typ
• časopisecké články MeSH

Gemmatimonas phototrophica AP64 is the first phototrophic representative of the bacterial phylum Gemmatimonadetes. The cells contain photosynthetic complexes with bacteriochlorophyll a as the main light-harvesting pigment and an unknown carotenoid with a single broad absorption band at 490 nm in methanol. The carotenoid was extracted from isolated photosynthetic complexes, and purified by liquid chromatography. A combination of nuclear magnetic resonance (1H NMR, COSY, 1H-13C HSQC, 1H-13C HMBC, J-resolved, and ROESY), high-resolution mass spectroscopy, Fourier-transformed infra-red, and Raman spectroscopy was used to determine its chemical structure. The novel linear carotenoid, that we have named gemmatoxanthin, contains 11 conjugated double bonds and is further substituted by methoxy, carboxyl and aldehyde groups. Its IUPAC-IUBMB semi-systematic name is 1'-Methoxy-19'-oxo-3',4'-didehydro-7,8,1',2'-tetrahydro- Ψ, Ψ carotene-16-oic acid. To our best knowledge, the presence of the carboxyl, methoxy and aldehyde groups on a linear C40 carotenoid backbone is reported here for the first time.

• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH

Light-harvesting capacity was investigated in six species of aerobic anoxygenic phototrophic (AAP) bacteria using absorption spectroscopy, fluorescence emission spectroscopy, and pigment analyses. Aerobically grown AAP cells contained approx. 140-1800 photosynthetic reaction centers per cell, an order of magnitude less than purple non-sulfur bacteria grown semiaerobically. Three of the studied AAP species did not contain outer light-harvesting complexes, and the size of their reaction center core complexes (RC-LH1 core complexes) varied between 29 and 36 bacteriochlorophyll molecules. In AAP species containing accessory antennae, the size was frequently reduced, providing between 5 and 60 additional bacteriochlorophyll molecules. In Roseobacter litoralis, it was found that cells grown at a higher light intensity contained more reaction centers per cell, while the size of the light-harvesting complexes was reduced. The presented results document that AAP species have both the reduced number and size of light-harvesting complexes which is consistent with the auxiliary role of phototrophy in this bacterial group.

• Klíčová slova
• Bacterial photosynthesis, Bacteriochlorophyll, Photosynthetic unit size, Purple non-sulfur bacteria, Reaction center core complex,
• MeSH
• aerobióza MeSH
• Alphaproteobacteria chemie   metabolismus   MeSH
• bakteriochlorofyly metabolismus   MeSH
• fotosyntetická reakční centra (proteinové komplexy) chemie   metabolismus   MeSH
• fototrofní procesy MeSH
• Gammaproteobacteria chemie   metabolismus   MeSH
• světlosběrné proteinové komplexy chemie   metabolismus   MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• bakteriochlorofyly MeSH
• fotosyntetická reakční centra (proteinové komplexy) MeSH
• světlosběrné proteinové komplexy MeSH