Rhodospirillum rubrum structure

Schneider, G., Lindqvist, Y., Lundqvlst, T. Crystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7 A resolution. J. Mol. Biol. 

Drennan CL, J Heo, MD Sintchak, E Schreiter, PW Ludden (2001) Life on carbon monoxide x-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase. Proc Natl Acad Sci USA 98 11973-11978. 

A. Planchard, L. Mignot, T. Jouenne, G.-A. Junter (1984) Photoproduction of molecular hydrogen by Rhodospirillum rubrum immobilized in composite agar layer/microorous membrane structures. Appl. Microbiol. Biotechnol., 31 49-54... 

Three-dimensional structure of ribulose-l,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9 A resolution. EMBO J. 5, 3409-3415. 

As an example of an asymmetric membrane integrated protein, the ATP synthetase complex (ATPase from Rhodospirillum Rubrum) was incorporated in liposomes of the polymerizable sulfolipid (22)24). The protein consists of a hydrophobic membrane integrated part (F0) and a water soluble moiety (Ft) carrying the catalytic site of the enzyme. The isolated ATP synthetase complex is almost completely inactive. Activity is substantially increased in the presence of a variety of amphiphiles, such as natural phospholipids and detergents. The presence of a bilayer structure is not a necessary condition for enhanced activity. Using soybean lecithin or diacetylenic sulfolipid (22) the maximal enzymatic activity is obtained at 500 lipid molecules/enzyme molecule. With soybean lecithin, the ATPase activity is increased 8-fold compared to a 5-fold increase in the presence of (22). There is a remarkable difference in ATPase activity depending on the liposome preparation technique (Fig. 41). If ATPase is incorporated in-... 

Monomeric intermediates during the assembly of oligomeric proteins are usually inactive and the formation of native quaternary structures are often a prerequisite for catalytic activity. One clear reason for this is that the active sites of some enzymes are located at the interface between subunits and are formed by amino acid residues from different subunits. Such examples are aspartate transcarbamoylase from K coli5) and ribulose bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum.6)... 

D. Fotiadis, P. Qian, A. Philippsen, P.A. Bullough, A. Engel, C.N. Hunter, Structural analysis of the reaction center light-harvesting complex I photosynthetic core complex of Rhodospirillum rubrum using atomic force microscopy. J. Biol. Chem. 279, 2063-2068 (2004)... 

Table 1 summarizes the general characteristics of representative urease, hydrogenase and CODHs. As it will be further discussed below, the X-ray structures of only two Ni-containing proteins, urease and hydrogenase, are known [16, 17]. The former has the well known triose phosphate isomerase (TIM) barrel topology (Fig. 1) whereas the latter displays a so far unique folding (Fig. 2). The next challenge will be the elucidation of the crystal structures of the CODH/ACS enzyme of Clostridium thermoaceticum and of the simpler CODH from Rhodospirillum rubrum. 

Wiemken V and Bachofen R (1984) Probing the smallest functional unit of the reaction center of Rhodospirillum rubrum G-9 with proteinoses. FEBS Lett 166 155-159 Williams JC, Alden RG, Murchison HA, Peloquin JM, Woodbury NW and Allen IP (1992) Effects of mutations near the bacteriochlorophylls in reaction centers from Rhodobacter sphaeroides. Biochemistry 31 11029-11037 Yeates TO, Komiya H, Chirino A, Rees DC, Allen IP and Feher G (1988) Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1 Protein-cofactor bacterio-chlorophyll bacteriopheophytin and carotenoid interactions. Proc Natl Acad Sci USA 85 7993-7997 Zinth W, Knapp EW, Fischer SF, Kaiser W, Deisenhofer J and Michel H (1985) Correlation of structural and spectroscopic properties of a photo synthetic reaction center. Chem Phys Lett 119 1 ... 

Heterologous reconstitution experiments show some structural restraints Spheroidene from Rb. sphaeroides can be reconstituted into a complex with LHl polypeptides from Rhodospirillum rubrum, restoring spectral properties of native Rs. rubrum LHl and carotenoid-BChl energy transfer whereas spirilloxanthin is unable to incorporate into a reconstituted complex with LHl apoproteins from Rb. sphaeroides (Davis et al., 1995). 

Boucher F, van der Rest M and Gingras G (1977) Structure and function of carotenoids in the photoreaction center from Rhodospirillum rubrum. Biochi m Biophys Acta 461 339-357... 

For example, incorporation of nickel into carbon monoxide dehydrogenase of Rhodospirillum rubrum requires the prior reduction of an Fe-S cluster. Structural studies of this protein reveal that the added Ni completes a unique [lNi-4Fe-4S] center that is required for activity.Another example of a reductive activation step occurs during NiFe-hydrogenase biosynthesis, perhaps involving participation of the Fe-S cluster in HypD. Yet a third example from the Ni-enzyme literature involves the synthesis of methyl-X-coenzyme M reductase, a methanogen enzyme that contains the Ni-tetrapyrrole cofactor F43q. Formation of active enzyme requires both the reduction of Ni + to NF+ and reduction of a C=N bond in the organic macrocycle. 

Barber, J. (1982). Influence of surface charges on thylakoid structure and function. Ann. Rev. Plant Physiol. 33 261-295 Loach, P.A., Parkes, P.S., Bustamante, P. (1984). Regulation of photosynthetic unit structure in Rhodospirillum rubrum whole cells. In Sybesma C. (ed) Adv. Photosynth. Res. vol II. 189-197 Holmes, N.G. and Allen, J.F. (1986). Protein phosphorylation as a control for excitation energy transfer in Rhodospirilium rubrum. FEBS Lett. 200 144-148... 

In Rhodobacter sphaeroides and Rhodospirillum rubrum, a new type of antenna Bchl-form whose energy level is lower than that of the special pair Bchl of the reaction center (RC) has been reported (4-6). Such components should be surveyed in other photosynthetic bacteria to account for the functional role and structural basis for the specific energy level. 

STRUCTURAL COMPARISON BETWEEN RHODOSPIRILLUM RUBRUM PLASMID AND CHLOROPLAST DNA... 

Boatman, E.S. (1964) Observations on the fine structure of spheroplasts of Rhodospirillum rubrum. J. Cell Biol., 20, 297-311. 

Laser-microwave spectroscopy was also reported of the triplet state of photosynthetic bacteria, namely, of Rhodospirillum rubrum, Rhodo-pseudomonas spheroides, and Chromaticum vinosum, in chemically reduced cellular preparations at 2 K. The authors found similarities of the triplet state frequencies, spectral features, and intersystem crossing rates that suggest that the reaction centers in photosynthetic bacteria possess a common structure. 

Davis CM, Parkes-Loach PS, Cook CK, Meadows KA, Bandilla M, Scheer H, and Loach PA. Comparison of the structural requirements for bacteriochlorophyll binding in the core light-harvesting complexes of Rhodospirillum rubrum and Rhodobacter sphaeroides using reconstitution methodology with bacteriochlorophyll analogs. Biochemistry 1996 35 3072-3084. 

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