Disease relevance of Rhodospirillum

• With the publication this year of the crystal structure of the LH2 complex from Rhodopseudomonas acidophila and the projection structure of the LH1 complex from Rhodospirillum rubrum, structural models now exist for all the components in the bacterial photosynthetic apparatus [1].
• The nitrogenase-regulating enzymes dinitrogenase reductase ADP-ribosyltransferase (DRAT) and dinitrogenase reductase-activating glycohydrolase (DRAG), from Rhodospirillum rubrum, were shown to be sensitive to the redox status of the [Fe(4)S(4)](1+/2+) cluster of nitrogenase Fe protein from R. rubrum or Azotobacter vinelandii [2].
• Ribulose-bisphosphate carboxylases from the cyanobacterium Synechococcus PCC 6301 and the bacterium Rhodospirillum rubrum also catalyzed pyruvate formation and to the same extent as the spinach enzyme [3].
• Three crystal forms of the dimeric form of the enzyme ribulose-1,5-bisphosphate carboxylase from the photosynthetic bacterium Rhodospirillum rubrum have been obtained from the gene product expressed in Escherichia coli [4].
• The sequence belongs to the same class as the published Alcaligenes and Rhodospirillum rubrum cytochrome c' squences, but the resemblance is not close [5].

High impact information on Rhodospirillum

• Here we compare crystallographically independent subunits of the dimeric cytochrome c' from the bacterium Rhodospirillum molischianum to examine how lattice effects influence refined B-values [6].
• Activating factor for the iron protein of nitrogenase from Rhodospirillum rubrum [7].
• Here we describe the cloning and sequencing of the genes encoding the PYPs from E.halophila SL-1 (type strain) and Rhodospirillum salexigens [8].
• Comparison of the crystal structures of the L2 and L8S8 forms of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum and spinach respectively, reveals a remarkable similarity in the overall architecture of the L2 building blocks in the two enzymes [9].
• However, the PYP domain (Ppr-PYP) from the sensor histidine kinase Ppr in Rhodospirillum centenum, which regulates the catalytic activity of Ppr by blue light absorption, may allow such issues to be addressed [10].

Chemical compound and disease context of Rhodospirillum

• An inactive, Ni-deficient form of carbon monoxide (CO) dehydrogenase [carbon-monoxide:(acceptor) oxidoreductase; EC 1.2.99.2], designated apo-CO dehydrogenase, accumulated in Rhodospirillum rubrum when cells were grown in the absence of Ni and treated with CO [11].
• Covalent modification of the iron protein of nitrogenase from Rhodospirillum rubrum by adenosine diphosphoribosylation of a specific arginine residue [12].
• During the activation of the inactive dinitrogenase reductase from Rhodospirillum rubrum, an adenine-like molecules is lost and phosphate is found on both active and inactive forms of the protein [13].
• We recently showed that in the LH1 complex of the purple bacterium Rhodospirillum rubrum, which is rather inefficient in carotenoid-to-BChl energy transfer, a third additional carotenoid excited singlet state is formed [14].
• This gene is evolutionarily conserved and shows significant amino acid homologies to mouse and human purine nucleoside phosphorylases and to a hypothetical 25.8-kDa protein in the pet gene (coding for cytochrome bc1 complex) region of Rhodospirillum rubrum [15].

Biological context of Rhodospirillum

• 2-(4-Bromoacetamido)anilino-2-deoxypentitol 1,5-bisphosphate, a new affinity label for ribulose bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum. Determination of reaction parameters and characterization of an active site peptide [16].
• ADP-ribosylarginine hydrolases from mammalian tissues and Rhodospirillum rubrum exhibit three regions of similarity in deduced amino acid sequence [17].
• ATP synthesis and hydrolysis by Rhodospirillum rubrum chromatophores as well as the soluble RrF1-ATPase activity are inhibited by 4-chloro-7-nitrobenzofurazan (NBD-C1) in a dithiothreitol-reversible manner [18].
• Partition kinetics of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum [19].
• A B800-850 light-harvesting complex (also called LH2) deficient strain of Rhodospirillum molischianum was constructed by replacing a portion of the LH2 gene cluster by a kanamycin resistance gene cartridge [20].

Anatomical context of Rhodospirillum

• Surface-enhanced resonance Raman scattering spectroscopy of bacterial photosynthetic membranes. The carotenoid of Rhodospirillum rubrum [21].
• Component of the Rhodospirillum centenum photosensory apparatus with structural and functional similarity to methyl-accepting chemotaxis protein chemoreceptors [22].
• Cell-cycle-specific fluctuation in cytoplasmic membrane composition in aerobically grown Rhodospirillum rubrum [23].
• A hybrid ATPase composed of cloned chloroplast ATP synthase beta and gamma subunits (betaC and gammaC) and the cloned alpha subunit from the Rhodospirillum rubrum ATP synthase (alphaR) was assembled using solubilized inclusion bodies and a simple single-step folding procedure [24].
• A unique Trp residue in the recombinant dIII component of transhydrogenase from human heart mitochondria (hsdIII), and an equivalent Trp engineered into the dIII component of Rhodospirillum rubrum transhydrogenase (rrdIII.D155W), are more fluorescent when NADP(+) is bound to the proteins, than when NADPH is bound [25].

Gene context of Rhodospirillum

• This vector was utilized for the construction of a cyanobacterial rbc null mutant in which the entire sequence comprising both rbc genes, was replaced by the Rhodospirillum rubrum rbcL gene linked to a chloramphenicol resistance gene [26].
• We demonstrate, by modeling the structure using the highly homologous structure of LH2 from Rhodospirillum molischianum, that it has the minimal size for BChl binding [27].
• Additionally, we have compared the self-assembly of sphbeta31 and LH1beta24 with BChls and discovered that the association enthalpies and entropies of both species are similar to those measured for native LH1 from Rhodospirillum rubrum [27].
• We propose that Rhodospirillum rubrum is a naturally occurring bchP mutant and that an insertion mutation may have been the initial cause of a partial loss of function [28].
• The low-lying excited states of a B850 ring of Rhodospirillum (Rs.) molischianum are determined accurately by a semiempirical INDO/S method [29].

Analytical, diagnostic and therapeutic context of Rhodospirillum

• Functional analysis of the putative catalytic bases His-321 and Ser-368 of Rhodospirillum rubrum ribulose bisphosphate carboxylase/oxygenase by site-directed mutagenesis [30].
• A reaction center-light-harvesting 1 complex (RC-LH1) from a Rhodospirillum rubrum mutant with altered esterifying pigments: characterization by optical spectroscopy and cryo-electron microscopy [31].
• The contribution of the carotenoid to the visible circular dichroism of the light-harvesting antenna of Rhodospirillum rubrum [32].
• Antiserum against component 2 Rhodospirillum rubrum nitrogenase was found to cross-react with component 2 from strain 227, and Western immunoblots using this antiserum showed no evidence for covalent modification of component 2 [33].
• The carbon monoxide dehydrogenase from the photosynthetic bacterium Rhodospirillum rubrum was purified over 600-fold by DEAE-cellulose chromatography, heat treatment, hydroxylapatite chromatography, and preparative scale gel electrophoresis [34].

References