Rhodospirillum rubrum differences

Tim Steinbuchel (1990) studied the mechanisms of Alcaligenes spp. and Rhodospirillum rubrum for PHB synthesis by using butyric acid. Later, Steinbuchel (1991) confirmed the results for the potential of PHAs production and the compositions of PHAs. Under various microbial strains used, different contents of PHAs were obtained. 

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-... 

The Mg2+-activated ATPase (or ATP synthase) is made up of two parts. The Fj component is the catalytic, Mg2+-binding, extrinsic membrane protein composed of five different subunits, a, (3, y, S and e. The F0 component is an intrinsic membrane complex that contains three subunits, a, b and c, and mediates proton translocation. The F, protein is bound to the membrane through interaction with F0. The complexity of the F,F0 enzyme has presented many difficulties. Hie greatest advances have been made for the bacterial enzymes, notably for thermophiles, Escherichia coli and Rhodospirillum rubrum, where progress has been made in the purification of subunits and their reconstitution into membranes, and the identification of binding sites for Mg2+ and nucleotides on the Fi subunits.300 FiF0 preparations can be incorporated into liposomes and display H+ translocation, ATP-P, exchange and ATP synthesis.301... 

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)... 

Carbon monoxide dehydrogenase/acetyl coenzyme A synthase (CODH/ACS) describes two different classes of enzymes carbon monoxide dehydrogenase (CODH) isolated from Rhodospirillum rubrum or Carboxydothermus hydrogenoformans reversibly oxidizes CO to CO2 according to equation (2), and the bifunctional CODH/ACS enzyme from Moorella thermoacetica catalyzes the reversible reduction of CO2 to CO (CODH) and acetyl coenzyme assembly/disassembly (ACS) (equation 3). ... 

Fig. 4. Difference absorption spectrum of photoreduced bacleriopheophytin (B

A comparison of CD spectra (200—600 nm) between bovine heart fenicytochrome c and ferricytochrome from Rhodospirillum rubrum showed marked differences, while the spectra were more similar in the reduced forms. These differences were attributed to subtle variations around the hemes rather than to differences in the polypeptide chain conformations (216). Optical activity studies of cytochromes C3 showed similarities among three species of Desulfovibrio but revealed differences from mammalian cytochrome c. Rotatory strengths of the resolved CD... 

Nuijs AM, van Bochove AC, Joppe HLP and Duysens LNM (1984) Picosecond carotenoid triplet formation in the antenna of Rhodospirillum rubrum as measured by absorbance difference spectroscopy. In Sybesma C (ed) Advances in Photosynthesis Research, Vol I, pp 65-68, Martinus Nijhoff Publishers, The Hague... 

Nuijs AM, van Grondelle R, Joppe HLP, van Bochove AC and Duysens LNM (1985) Singlet and triplet excited carotenoid and antenna bacteriochlorophyll ofthe purple photosynthetic bacterium Rhodospirillum rubrum as studied by picosecond absorbance difference spectroscopy. Biochim Biophys Acta 810 94-105... 

The genes for the catalytic part of the F F -ATPase from two different phototrophic bacteria have been sequenced Rhodospirillum rubrum (1) and Rhodopseudomonas blastica (2). The sequence of the genes for the F of R. rubrum is also known (3). The atp1-operon of the latter bacteria encodes the five subunits found in the preparations of the enzyme (Walker, J. E., Falk, G., and Strid, A., unpublished results) as judged by N-terminaT analysis. The atp-operon of Rps. blastica also contains a sixth gene, termed X. The F--protein has not previously been prepared from Rps. blas-tica. Some characteristic properties of a pure preparation of the enzyme is compared to the properties of the R. rubrum F. ... 

Furthermore, we report on a comparative investigation of D+ in RCs of different BChl g-containing purple bacteria. The EPR and ENDOR/TRIPLE experiments reveal significant differences in the spin density distribution of D+ in Rhodospirillum (Rs) rubrum, Rb. sphaeroides, and Rb. capsulatus. 

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