Rhodopseudomonas capsulatus

Figure 5. Essential amino acid patterns of proteins extracted from Spirulina maxima, Rhodopseudomonas capsulatus, and Trifolium repens L and those of plasteins produced from these proteins, with the FAO/WHO suggested pattern in each background (white)...

Iron nitrogenase. FeFe proteins (e.g. from Azotobacter vinelandii and Rhodopseudomonas capsulatus) are hexameric (02 2 2) actually contain low... 

Reduction of dimethyl sulfoxide and trimethylamine-fV-oxide by Rhodobacter capsulatus (Rhodopseudomonas capsulata) (King et al. 1987)... 

The larger part of research on light-driven eleetron transfer in purple photosynthetic bacteria has involved three speeies, Rhodopseudomonas (Rps.) viridis, Rhodobacter (Rb.) sphaeroides and Rb. capsulatus. The bulk of this article is written in reference to the Rb. sphaeroides reaetion eentre, the subject of the majority of spectroscopic and mutagenesis work earried out to date. However, much of the research described below has involved the reaction centre from Rb. capsulatus or Rps. viridis, or reaetion eentres from other species of purple bacteria. 

Rhodobacter sphaeroides and Rhodobacter capsulatus were formerly classified in the genus Rho-dopseudomonas. They have recently been reclassified [23]. Rhodopseudomonas gelatinosa is now classified as Rhodocyclus gelatinosus. 

Aerobic bacteria such as Azotobacter vinelandii, Alcaligenes eutrophus, and Nocardia opaca, and facultative anaerobes, such as Escherichia coli and various species of Rhizobium and Bradyrhizobium (the symbionts of leguminous plants), also contain hydrogenase, as do photosynthetic bacteria such as Chromatium vinosum, Rhodobacter capsulatus (formerly Rhodopseudomonas capsulata), and Anabaena variabilis (a filamentous cyanobacterium). The thermophilic hydro-... 

The acceptor side of the PS II reaction center is structurally and functionally homologous to the reducing side of reaction centers from a number of photosynthetic bacteria, including Rhodopseudomonas viridis. Rhodobacter sphaeroides and capsulatus. and Chloroflexus aurantiacus. The reaction center complexes of viridis and sphaeroides have been crystallized, and the three-dimensional structure of these has been determined at high resolution [3-7]. With the exception of (a) the His residues in the bacterial reaction center that serve as ligands to the Mg of the accessory bacteriochlorophylls, and (b) the Glu residue that serves as a ligand to the non-heme iron between and Q0, all of the amino acid residues that function as important... 

Despite the fact that photosynthetic PPi formation only has been revealed in R. rubrum it is plausible to suggest that other phototro-phic bacteria would be capable of catalyzing PPi synthesis. Thus a membrane bound PPase has recently been found in Rhodopseudomonas pa-lustris (2,3). We have also examined the possibility of PPi synthesis in chromatophores from Rhodopseudomonas viridis. Rhodopseudomonas blastica and Rhodobacter capsulatus. 

A. Kreusch, and G. E. Schulz, Refined structure of the porin from Rhodopseudomonas blastica. Comparison with the porin from Rhodobacter capsulatus,j. Mol Biol, 243,891-905 (1994). 

Structural analysis of the quinone binding sites. Table 1 lists the amino acid residues that form the surface of the cavity in which each quinone is located in the purple bacteria Rhodopseudomonas virUis [7], R, sphaeroides [8,9], R. capsulatus [10], Rhodospirillum rubrum [11], and the green bacterium Chloroflexus aurantiacus [12,13]. 

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