Chlorobium tepidum

Synecnocystis Chlorobium tepidum Methylococcus capsulatus Rhodobacter capsulatus Rhosdospirillum rubrum Chloroflexus aurantiacus Fibrobacter succinogenes Thermoanaerobacter tengcongensis... 

Figure 23-28 (A) Model of a light-harvesting chlorosome from green photosynthetic sulfur bacteria such as Chlorobium tepidum and species of Prosthecochloris. The chlorosome is attached to the cytoplasmic membrane via a baseplate, which contains the additional antenna bacteriochlorophylls (795 BChl a) and is adjacent to the trimeric BChl protein shown in (B) and near the reaction center. After Li et al.302 and Remigy et a/.304 (B) Alpha carbon diagram of the polypeptide backbone and seven bound BChl a molecules in one subunit of the trimeric protein from the green photosynthetic bacterium Prosthecochloris. For clarity, the magnesium atoms, the chlorophyll ring substituents, and the phytyl chains, except for the first bond, are omitted. The direction of view is from the three-fold axis, which is horizontal, toward the exterior of the molecule. From Fenna and Matthews.305 See also Li et al.302...

Agrobacterium tumefaciens Brucella melitensis Burkholderia fungorum (2) Campylobacter jejuni Caulobacter crescentus Chlorobium tepidum Chloroflexus aurantiacus Deinococcus radiodurans Magnetospirillum magnetotacticum (2) Mesorhizobium loti (2) Methanosarcina acetivorans (2)b Methanosarcina mazei (2)b Mycobacterium tuberculosis Myxococcus xanthus Nostoc punctiforme (2)... 

Schmidt, K.A., Neerken, S., Permentier, H.P., Hager-Braun, C., and Amesz, J. (2000) Electron transfer in reaction center core complex from green sulfur bacteria Prosthecochloris aestuarii and Chlorobium tepidum, Biochemistry 39, 7212-7220. 

FIGURE 2.1 Model of the photosynthetic apparatus (Fenna-Matthews-Olson complex) in Chlorobium tepidum. SOURCE Donald A. Bryant, The Pennsylvania State University, and Dr. Niels-Ulrik Frigaard, University of Copenhagen. 

Figure 22. A representation of the aggregation shifts, i.e., the difference between the chemical shift in the aggregate (i.e., the solid state) and in the monomer (i.e., in solution), as determined for the H and 13C nuclei in a uniformly 13C enriched bacteriochlorophyll (BChl) c in intact chlorosomes of Chlorobium tepidum, using 2D H-13C and 3D H-13C-13C dipolar correlation spectroscopy at a magnetic field of 14.1 T. Circles correspond to upfield changes upon aggregation with the size of the circle indicating the magnitude of the change. The different representations in I and II correspond to the experimental observation of two separate components. (Reproduced with permission from ref 162. Copyright 2001 American Chemical Society.)...

Attempts to prepare pure reaction-center complexes from green sulfur bacteria have proven quite difficult in the past, and usually resulted in severely diminishing the photochemical activity of the preparation. However, the new preparative procedure of Francke et al has yielded RC-complexes that are photochemically active and reasonably pure. They resemble the core complex of photosystem 1, but only have 16 BChls a and 4 molecules of the Chl-a isomer, as subsequently determined by Griesbeck, Hager-Braun, Rogl and Hauska ° for the P840-reaction center from Chlorobium tepidum. 

N Kusumoto, K Inoue, FI Nasu and FI Sakurai (1994) Preparation of a photoactive reaction center complex containing photoreducible Fe-S centers and photooxidizable cytochrome c from the green sulfur bacterium Chlorobium tepidum. Plant Cell Physiol 35 17-25... 

C Griesbeck, C Flager-Braun, FI RogI and G Flauska (1998) Quantitation of P840 reaction center preparations from Chlorobium tepidum Chlorophylls and FMO-protein. Biochim Biophys Acta 1365 285-293... 

Fig. 10. Top Charge recombination reactions in photosystem I (left) and in the reaction center of green-sulfur bacteria (right). Bottom Flash-induced absorbance changes and kinetics of charge recombination in the dark. [The left panel is reproduced from Fig. 3 (A). Data in lower, right panel are taken from Kusumoto, Inoue and Sakurai (1995) Spectroscopic studies of bound cytochrome c and an iron-sulfur center in a purified reaction center from the green sulfur bacterium Chlorobium tepidum. Photosynthesis Res 43 109.

N Kusumoto, K Inoue and H Sakurai (1995) Spectroscopic studies of bound cytochrome c and an iron-sulfur center in a purified reaction center complex from the green sulfur bacterium Chlorobium tepidum. Photosynthesis Res 43 107-112... 

Takaichi S, Wang Z-Y, Umetsu M, Nozawa T, Shimada K and Madigan MT (1997a) New carotenoids from the thermophilic green sulfur bacterium Chlorobium tepidum r,2 -dihydro-y-carotene, l, 2 -dihydrochlorobactene, and OH-chlorobactene glucoside ester, and the carotenoid composition of different strains. Arch Microbiol 168 270-276... 

Bialek-Bylka GE, Fujii R, Chen C-H, Oh-oka H, Kamiesu A, Satoh K, Koike H and Koyama Y (1998b) 15-Cis-carotenoids found in the reaction center of a green sulfur bacterium Chlorobium tepidum and in the Photosystem I reaction center of a cyanobacterium Synechococcus vulcanus. Photosynth Res 58 1-8... 

Seo D, Sakuiai H (2002) Purification and characterization of FeiTedoxin-NAD(PX+) reductase from the green sulfur bacterium Chlorobium tepidum. Biochim Biophys Acta 1597 123 132... 

A new third family of functional lycopene cyclase CruA has been found in the green sulfur bacterium Chlorobaculum (previously Chlorobium) tepidum, and the main product of CruA is y-carotene 12 in Escherichia coli with a lycopene 7 background [34]. Homologous genes cruA and cruP have been found in the genome of Synechococcus sp. PCC 7002, and the main product of CruA and CruP is... 

Carotenoids of Chlorobaculum (previously Chlorobium) tepidum have been precisely investigated [85], and some enzymes involved in the synthesis of these carotenoids have been functionally confirmed (Fig. 106.6, Table 106.3) [31, 34, 79]. 

Frigaard N-U, Maresca JA, Yunker CE, Jraies AD, Bryant DA (2004) Genetic manipulation of carotenoid biosynthesis in the green sulfur bacterium Chlorobium tepidum. J Bacteriol 186 5210-5220... 

Maresca JA, Bryant DA (2006) Two genes encoding new carotenoid-modifying enzymes in the green sulfur bacterium Chlorobium tepidum. J Bacteriol 188 6217-6223 Komori M, Ghosh R, Takaichi S, Hu Y, Mizoguchi T, Koyama Y, Kuki M (1998) A null lesion in the rhodopin 3,4-desaturase of Rhoodspirillum rubrum unmasks a cryptic branch of the carotenoid biosynthetic pathway. Biochemistry 37 8987-8994... 

Camara-Artigas A, Blankenship RE, and Allen JP. The structure of the FMO protein from Chlorobium tepidum at 2.2 angstrom resolution. 

Remigy HW, Stahlberg H, Fotiadis D, Muller SA, Wolpensinger B, Engel A, Hauska G, and Tsiotis G. The reaction center complex firom the green sulfur bacterium Chlorobium tepidum A structural analysis by scanning transmission electron microscopy. J. Molec. Biol 1999 290 851-858. 

Montano GA, Bowen BP, LaBelle JT, Woodbury NW, Pizziconi VB, and Blankenship RE. Characterization of Chlorobium tepidum chlorosomes A... 

Fig. 14 Comparison of the absorption spectra of 3 j -[Et,Et]-BChl c in various solvents and in the natural chlorosomes. Green trace—solution in dichloromethane red trace—same solution after addition of suprastoichiometric amoimts of methanol blue trace—dichloromethane solution diluted into a large excess of n-hexane black trace— natural chlorosomes isolated from Chlorobium tepidum...

Agostiano, A., Catucci, L., Colafemmina, G., deUa Monica, M., and Scheer, H., Relevance of the phytyl chain of the chlorophylls on the lamellar phase formation and organization, Biophys.J., 84,189, 2000. Van Rossum, B.-J., Steensgaard, D.B., Mulder, EM., Boender, G.J., Schaffner, K., Holzwarth, A.R., and de Groot, H.J.M., A refined model of the chlorosomal antennae of the green bacterium Chlorobium tepidum from proton chemical shift constraints obtained with high-field two-dimensional and three-dimensional MAS NMR dipolar correlation. Biochemistry, 40, 1587, 2001. Hynninen, RH., Chemistry of chlorophylls modifications, in Chlorophylls, Scheer, H., Ed., CRC Press LLC, Boca Raton, FL, 1991, p. 145. 

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