The complete amino acid sequence of the antenna polypeptide B806‐866‐β from the cytoplasmic membrane of the green bacterium <i>Chloroflexus auranliacus</i>

Wechsler, Thomas; Brunisholz, René A.; Frank, Gerhard; Suter, Franz; Zuber, Herbert

doi:10.1016/0014-5793(87)81335-2

Cited by 38 publications

(14 citation statements)

References 15 publications

(9 reference statements)

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“…B808-866 complexes are composed of a-and b-polypeptides consisting of 53 (calculated molecular weight 5599 Da) and 44 (calculated molecular weight 4840 Da) amino acid residues, respectively (Wechsler et al 1987). The a and b subunits run separately at apparent molecular masses of $6 and $4 kDa in Tris-Tricine SDS-PAGE (Figure 1).…”

Section: Resultsmentioning

confidence: 99%

Purification and Characterization of the B808–866 Light-harvesting Complex from Green Filamentous Bacterium Chloroflexus aurantiacus

et al. 2005

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The integral membrane light-harvesting complex B808-866 from the thermophilic green filamentous bacterium Chloroflexus aurantiacus has been isolated and characterized. Reversed-phase HPLC analysis demonstrated that the number of bacteriochlorophyll (BChl) in the B808-866 antenna complex is 36 +/- 2 per reaction center. The main carotenoid type is gamma-carotene, and the molar ratio of BChl to carotenoid is 3:2. The steady-state absorption and fluorescence spectroscopy of the B808-866 complex are reminiscent of the well-studied LH2 peripheral antenna of purple bacteria, whereas the protein sequence and the circular dichroism spectrum of B808-866 is more similar to the LH1 inner core antenna. The efficiency of excitation transfer from carotenoid to BChl is about 25%. The above results combined with electron microscopy and dynamic light scattering analysis suggest that the B808-866 antenna is more like the LH1, whereas surrounds the reaction center but probably consists of 24 building blocks with a ring diameter of about 20 nm. The above results suggested that there are probably two reaction centers inside the ring of B808-866. The unique properties of this light-harvesting complex may provide insights on the protein-pigment interactions in bacterial photosynthesis.

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Section: Resultsmentioning

confidence: 99%

Purification and Characterization of the B808–866 Light-harvesting Complex from Green Filamentous Bacterium Chloroflexus aurantiacus

et al. 2005

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“…The protein sequence data confirm what kinetic and spectral measurements suggested several years ago, namely that the Chloroflexus reaction center is in essence closest to the purple bacterial reaction centers, but is less similar to any purple bacterial reaction center than all the purples are to each other (Bruce et al 1982, Pierson and Thornber 1983, Blankenship 1985, Shiozawa et al 1987, Kirmaier and Holten 1987, Ovchinnikov 1988a,b, Shiozawa et al 1989). Although the data sets are much less complete, there is also clear evidence for a reasonably close evolutionary relatedness between the purple bacteria and Chloroflexus when the membranebound bacteriochlorophyll a-containing antenna complexes (Wechsler et al 1985(Wechsler et al , 1987 and the membrane-bound cytochrome that donates electrons to the oxidized reaction center (Dracheva et al 1991) are examined. The significance of this disagreement between the evolutionary trees generated from 16S rRNA and the reaction center sequences is yet unclear.…”

Section: Sequence Analysis Of Pheophytin-quinone Reaction Centersmentioning

confidence: 99%

Origin and early evolution of photosynthesis

1992

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Photosynthesis was well-established on the earth at least 3.5 thousand million years ago, and it is widely believed that these ancient organisms had similar metabolic capabilities to modern cyanobacteria. This requires that development of two photosystems and the oxygen evolution capability occurred very early in the earth's history, and that a presumed phase of evolution involving non-oxygen evolving photosynthetic organisms took place even earlier. The evolutionary relationships of the reaction center complexes found in all the classes of currently existing organisms have been analyzed using sequence analysis and biophysical measurements. The results indicate that all reaction centers fall into two basic groups, those with pheophytin and a pair of quinones as early acceptors, and those with iron sulfur clusters as early acceptors. No simple linear branching evolutionary scheme can account for the distribution patterns of reaction centers in existing photosynthetic organisms, and lateral transfer of genetic information is considered as a likely possibility. Possible scenarios for the development of primitive reaction centers into the heterodimeric protein structures found in existing reaction centers and for the development of organisms with two linked photosystems are presented.

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“…The Chloroflexi contain a pheophytin-quinone type of reaction center similar to the reaction centers present in photosystem II and the purple phototrophic bacteria (11). The Chloroflexi also have a pigment-protein antenna complex called the B808-866 antenna protein, which is related to the LH1 complex that occurs in purple bacteria (41,42). In all species of green photosynthetic bacteria, the energy from absorbed photons is transferred down an energy gradient from the main chlorosome body to the chlorosome baseplate before it moves to the membranebound pigment-protein antenna complexes and then the reaction center.…”

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Initial Characterization of the Photosynthetic Apparatus of “ Candidatus Chlorothrix halophila,” a Filamentous, Anoxygenic Photoautotroph

et al. 2007

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"Candidatus Chlorothrix halophila" is a recently described halophilic, filamentous, anoxygenic photoautotroph (J. A. Klappenbach and B. K. Pierson, Arch. Microbiol. 181:17-25, 2004) that was enriched from the hypersaline microbial mats at Guerrero Negro, Mexico. Analysis of the photosynthetic apparatus by negative staining, spectroscopy, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that the photosynthetic apparatus in this organism has similarities to the photosynthetic apparatus in both the Chloroflexi and Chlorobi phyla of green photosynthetic bacteria. The chlorosomes were found to be ellipsoidal and of various sizes, characteristics that are comparable to characteristics of chlorosomes in other species of green photosynthetic bacteria. The absorption spectrum of whole cells was dominated by the chlorosome bacteriochlorophyll c (BChl c) peak at 759 nm, with fluorescence emission at 760 nm. A second fluorescence emission band was observed at 870 nm and was tentatively attributed to a membrane-bound antenna complex. Fluorescence emission spectra obtained at 77 K revealed another complex that fluoresced at 820 nm, which probably resulted from the chlorosome baseplate complex. All of these results suggest that BChl c is present in the chlorosomes of "Ca. Chlorothrix halophila," that BChl a is present in the baseplate, and that there is a membrane-bound antenna complex. Analysis of the proteins in the chlorosomes revealed an ϳ6-kDa band, which was found to be related to the BChl c binding protein CsmA found in other green bacteria. Overall, the absorbance and fluorescence spectra of "Ca. Chlorothrix halophila" revealed an interesting mixture of photosynthetic characteristics that seemed to have properties similar to properties of both phyla of green bacteria when they were compared to the photosynthetic characteristics of Chlorobium tepidum and Chloroflexus aurantiacus.

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The complete amino acid sequence of the antenna polypeptide B806‐866‐β from the cytoplasmic membrane of the green bacterium Chloroflexus auranliacus

Cited by 38 publications

References 15 publications

Purification and Characterization of the B808–866 Light-harvesting Complex from Green Filamentous Bacterium Chloroflexus aurantiacus

Purification and Characterization of the B808–866 Light-harvesting Complex from Green Filamentous Bacterium Chloroflexus aurantiacus

Origin and early evolution of photosynthesis

Initial Characterization of the Photosynthetic Apparatus of “ Candidatus Chlorothrix halophila,” a Filamentous, Anoxygenic Photoautotroph

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