Rhodospirillum rubrum ATCC 11170


Alias: Rhodospirillum rubrum S1, Rhodospirillum rubrum str. ATCC 11170, Rhodospirillum rubrum strain ATCC 11170

Top Publications

  1. Yasui M, Harada S, Kai Y, Kasai N, Kusunoki M, Matsuura Y. Three-dimensional structure of ferricytochrome c' from Rhodospirillum rubrum at 2.8 A resolution. J Biochem. 1992;111:317-24 pubmed
    ..One end of the bundle, in which a covalently bound protoheme IX prosthetic group is incorporated, is more divergent than the other.(ABSTRACT TRUNCATED AT 250 WORDS) ..
  2. Schneider G, Lindqvist Y, Lundqvist T. Crystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7 A resolution. J Mol Biol. 1990;211:989-1008 pubmed
    ..Crystallographic refinement at 1.7 A resolution clearly revealed the presence of a cis-proline at the active site. This residue is part of the highly conserved region Lys166-Pro167-Lys168. ..
  3. Sundaresan V, Yamaguchi M, Chartron J, Stout C. Conformational change in the NADP(H) binding domain of transhydrogenase defines four states. Biochemistry. 2003;42:12143-53 pubmed
    ..Because these states are distinguished by protein conformation and by net charge they may be important in the proton translocating mechanism of intact TH. ..
  4. Lundqvist T, Schneider G. Crystal structure of the binary complex of ribulose-1,5-bisphosphate carboxylase and its product, 3-phospho-D-glycerate. J Biol Chem. 1989;264:3643-6 pubmed
    ..The carboxyl group interacts with the side chains of His-287, Lys-191, and Asn-111. Implications of the activation process for the binding of 3-phosphoglycerate are discussed. ..
  5. Dus K, Sletten K, Kamen M. Cytochrome c2 of Rhodospirillum rubrum. II. Complete amino acid sequence and phylogenetic relationships. J Biol Chem. 1968;243:5507-18 pubmed
  6. Ideguchi T, Hu C, Kim B, Nishise H, Yamashita J, Kakuno T. An open reading frame in the Rhodospirillum rubrum plasmid, pKY1, similar to algA, encoding the bifunctional enzyme phosphomannose isomerase-guanosine diphospho-D-mannose pyrophosphorylase (PMI-GMP). Biochim Biophys Acta. 1993;1172:329-31 pubmed
  7. Johnson T, Yee B, Carlson D, Buchanan B, Johnson R, Mathews W, et al. Thioredoxin from Rhodospirillum rubrum: primary structure and relation to thioredoxins from other photosynthetic bacteria. J Bacteriol. 1988;170:2406-8 pubmed
    ..The results indicate that R. rubrum has an NADP-thioredoxin system similar to that of other photosynthetic purple bacteria. ..
  8. Brondijk T, van Boxel G, Mather O, Quirk P, White S, Jackson J. The role of invariant amino acid residues at the hydride transfer site of proton-translocating transhydrogenase. J Biol Chem. 2006;281:13345-54 pubmed
  9. Singh A, Venning J, Quirk P, van Boxel G, Rodrigues D, White S, et al. Interactions between transhydrogenase and thio-nicotinamide Analogues of NAD(H) and NADP(H) underline the importance of nucleotide conformational changes in coupling to proton translocation. J Biol Chem. 2003;278:33208-16 pubmed
    ..This might be a consequence of restricted rotation of the 3-carbothiamide group during the conformational change. ..

More Information


  1. Spangler N, Meyers M, Gierke K, Kerby R, Roberts G, Ludden P. Substitution of valine for histidine 265 in carbon monoxide dehydrogenase from Rhodospirillum rubrum affects activity and spectroscopic states. J Biol Chem. 1998;273:4059-64 pubmed
    ..This indicates that the electronic properties of center C have been modified possibly by the disruption or alteration of the ligand-mediated interaction between the nickel site and Fe4S4 chromophore. ..
  2. Zhang Y, Cummings A, Burris R, Ludden P, Roberts G. Effect of an ntrBC mutation on the posttranslational regulation of nitrogenase activity in Rhodospirillum rubrum. J Bacteriol. 1995;177:5322-6 pubmed
    ..rubrum. The expression of glutamine synthetase, as well as its posttranslational regulation, was also altered in this ntrBC mutant. ..
  3. Mather O, Singh A, van Boxel G, White S, Jackson J. Active-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase. Biochemistry. 2004;43:10952-64 pubmed
  4. Fraij B, Hartman F. Isolation and sequencing of an active-site peptide from Rhodospirillum rubrum ribulosebisphosphate carboxylase/oxygenase after affinity labeling with 2-[(bromoacetyl)amino]pentitol 1,5-bisphosphate. Biochemistry. 1983;22:1515-20 pubmed
    ..Sequence homology with the carboxylase/oxygenase from spinach indicates that the lysyl residue immediately preceding the alkylated methionine corresponds to Lys-334, a residue previously implicated at the active site. ..
  5. Romero I, GarcĂ­a Contreras R, Celis H. Rhodospirillum rubrum has a family I pyrophosphatase: purification, cloning, and sequencing. Arch Microbiol. 2003;179:377-80 pubmed
    ..rubrum is not sufficient for a normal growth rate, whereas the cytoplasmic enzyme is essential for growth. The characteristics of the gene and the encoded protein fit those of prokaryotic family I pyrophosphatases. ..
  6. van Boxel G, Quirk P, Cotton N, White S, Jackson J. Glutamine 132 in the NAD(H)-binding component of proton-translocating transhydrogenase tethers the nucleotides before hydride transfer. Biochemistry. 2003;42:1217-26 pubmed
    ..This ensures that hydride transfer is properly gated and does not take place in the absence of proton translocation. ..
  7. Andralojc P, Harris D. Isolation and characterisation of a functional alpha beta heterodimer from the ATP synthase of Rhodospirillum rubrum. FEBS Lett. 1992;310:187-92 pubmed
    ..The Vmax and Km (ATP) for this Mg(2+)-dependent activity were 110 +/- 10 nmol.min-1.mg protein-1 and 100 +/- 30 microM, respectively. The Km did not differ significantly from that of RF1. ..
  8. Williams R, Cotton N, Thomas C, Jackson J. Cloning and sequencing of the genes for the proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum and the implications for the domain structure of the enzyme. Microbiology. 1994;140 ( Pt 7):1595-604 pubmed
    ..It is suggested that this protease-sensitive region separates two subdomains and that, after trypsinolysis, at least one retains structural integrity and can dock with domains II and/or III. ..
  9. Baltscheffsky M, Brosché M, Hultman T, Lundvik L, Nyren P, Sakai Nore Y, et al. A 3-hydroxy-3-methylglutaryl-CoA lyase gene in the photosynthetic bacterium Rhodospirillum rubrum. Biochim Biophys Acta. 1997;1337:113-22 pubmed
    ..In addition, HMG-CoA lyase activity was found in R. rubrum cells grown anaerobically in the light with leucine as the carbon source. ..
  10. Meyer T, Ambler R, Bartsch R, Kamen M. Amino acid sequence of cytochrome c' from the purple photosynthetic bacterium Rhodospirillum rubrum S1. J Biol Chem. 1975;250:8416-21 pubmed
    The amino acid sequence of cytochrome c' from the purple photosynthetic bacterium Rhodospirillum rubrum S1 has been determined and is consistent with homology to cytochrome c' from the nonphotosynthetic bacterium Alcaligenes sp...
  11. Berard J, Belanger G, Corriveau P, Gingras G. Molecular cloning and sequence of the B880 holochrome gene from Rhodospirillum rubrum. J Biol Chem. 1986;261:82-7 pubmed
    ..rubrum is low, showing no evolutionary relatedness. This is in contrast to the high interspecific homology between the corresponding sequences of Rs. rubrum and Rhodopseudomonas capsulata B880 genes. ..
  12. Falk G, Walker J. DNA sequence of a gene cluster coding for subunits of the F0 membrane sector of ATP synthase in Rhodospirillum rubrum. Support for modular evolution of the F1 and F0 sectors. Biochem J. 1988;254:109-22 pubmed
    ..rubrum. The finding that genes for the F0 and F1 sectors of the enzyme are in separate clusters supports the view that these represent evolutionary modules. ..
  13. Belogurov G, Turkina M, Penttinen A, Huopalahti S, Baykov A, Lahti R. H+-pyrophosphatase of Rhodospirillum rubrum. High yield expression in Escherichia coli and identification of the Cys residues responsible for inactivation my mersalyl. J Biol Chem. 2002;277:22209-14 pubmed
    ..These data suggest a specific link between the incidence of Cys at positions 222 and 573 and the K(+) dependence of H(+)-PPase. ..
  14. Hartman F, Stringer C, Lee E. Complete primary structure of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum. Arch Biochem Biophys. 1984;232:280-95 pubmed
    ..Despite the low overall homology, striking homology between the two species of enzyme is observed in those regions previously implicated at the catalytic and activator sites. ..
  15. Lundqvist T, Schneider G. Crystal structure of the complex of ribulose-1,5-bisphosphate carboxylase and a transition state analogue, 2-carboxy-D-arabinitol 1,5-bisphosphate. J Biol Chem. 1989;264:7078-83 pubmed
    ..The binding of the transition state analogue to the nonactivated enzyme is different from the binding of the analogue to activated spinach ribulose-bisphosphate carboxylase. ..
  16. Jeeves M, Smith K, Quirk P, Cotton N, Jackson J. Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum. Biochim Biophys Acta. 2000;1459:248-57 pubmed
    ..The results are compared with the recently determined, high-resolution crystal structures of human and bovine dIII which also show the reversed nucleotide orientation. ..
  17. Soderlind E, Schneider G, Gutteridge S. Substitution of ASP193 to ASN at the active site of ribulose-1,5-bisphosphate carboxylase results in conformational changes. Eur J Biochem. 1992;206:729-35 pubmed
    ..The observed structural changes at the active site of the enzyme provide a molecular explanation for the differing behaviour of the Asp193----Asn mutant with respect to activation. ..
  18. Von Sternberg R, Yoch D. Molecular cloning and sequencing of the ferredoxin I fdxN gene of the photosynthetic bacterium Rhodospirillum rubrum. Biochim Biophys Acta. 1993;1144:435-8 pubmed
    ..R. rubrum FdI synthesis was stimulated by nif derepressing conditions, but was not completely repressed by nif repression. Previous reports of an extracellular clostridial-type ferredoxin in R. rubrum could not be confirmed. ..
  19. Self S, Hunter C, Leatherbarrow R. Molecular cloning, sequencing and expression of cytochrome c2 from Rhodospirillum rubrum. Biochem J. 1990;265:599-604 pubmed
    ..Evidence is presented for the production of assembled cytochrome c2 in Escherichia coli, but recombinants grow poorly and are unstable, suggesting toxicity of the gene product in this organism. ..
  20. Lindblad A, Jansson J, Brostedt E, Johansson M, Hellman U, Nordlund S. Identification and sequence of a nifJ-like gene in Rhodospirillum rubrum: partial characterization of a mutant unaffected in nitrogen fixation. Mol Microbiol. 1996;20:559-68 pubmed
    ..By primer extension, the initiation site for transcription was located, and a typical sigma 54 promoter sequence was identified. ..
  21. Johansson M, Nordlund S. Transcription of the glnB and glnA genes in the photosynthetic bacterium Rhodospirillum rubrum. Microbiology. 1996;142 ( Pt 5):1265-72 pubmed
    ..The total level of the two transcripts was much higher in nitrogen-fixing cells than in ammonia-grown cells. ..
  22. Sedelnikova S, Burke J, Buckley P, Rice D, Jackson J, Cotton N, et al. Crystallization of the dI component of transhydrogenase, a proton-translocating membrane protein. Acta Crystallogr D Biol Crystallogr. 2000;56:1170-2 pubmed
    ..A full structure determination will lead to important information on the mode of action of this proton pump and will permit the comparison of the structure-function relationships of dI with those of alanine dehydrogenase. ..
  23. Yamaguchi M, Hatefi Y. Energy-transducing nicotinamide nucleotide transhydrogenase: nucleotide sequences of the genes and predicted amino acid sequences of the subunits of the enzyme from Rhodospirillum rubrum. J Bioenerg Biomembr. 1994;26:435-45 pubmed
    ..rubrum enzyme (139 residues; molecular weight 14888) has considerable sequence identity in its C-terminal half to the corresponding segments of the bovine and the alpha subunit of the E. coli transhydrogenases. ..
  24. Theiler R, Suter F, Zuber H. N-terminal sequences of subunits L and M of the photosynthetic reaction centre from Rhodospirillum rubrum G-9+. Separation of the subunits by gel filtration on hydroxypropylated Sephadex G 100 in organic solvents. Hoppe Seylers Z Physiol Chem. 1983;364:1765-76 pubmed
    ..The homology among subunits L is close to 90% and thus markedly higher than that among subunits M (32%). This finding indicates a pre-eminent role of subunit L in the primary events of photosynthetic energy conversion. ..
  25. Sundaresan V, Chartron J, Yamaguchi M, Stout C. Conformational diversity in NAD(H) and interacting transhydrogenase nicotinamide nucleotide binding domains. J Mol Biol. 2005;346:617-29 pubmed
  26. Wang Z, Gokan K, Kobayashi M, Nozawa T. Solution structures of the core light-harvesting alpha and beta polypeptides from Rhodospirillum rubrum: implications for the pigment-protein and protein-protein interactions. J Mol Biol. 2005;347:465-77 pubmed
  27. Falk G, Hampe A, Walker J. Nucleotide sequence of the Rhodospirillum rubrum atp operon. Biochem J. 1985;228:391-407 pubmed
    ..However, as in the related organism Rhodopseudomonas blastica, neither genes for components of F0, the membrane sector of ATP synthase, nor a homologue of the E. coli uncI gene are associated with this locus, as they are in E. coli. ..
  28. Belanger G, Berard J, Corriveau P, Gingras G. The structural genes coding for the L and M subunits of Rhodospirillum rubrum photoreaction center. J Biol Chem. 1988;263:7632-8 pubmed
    ..Interspecies evolutionary distance is greater for pufL than for pufM. ..
  29. Majewski C, Trebst A. The pet genes of Rhodospirillum rubrum: cloning and sequencing of the genes for the cytochrome bc1-complex. Mol Gen Genet. 1990;224:373-82 pubmed
    ..The similarity of the deduced amino acid sequence of the three subunits to the corresponding subunits of other organisms is described and implications for structural features of the subunits are discussed. ..
  30. Bhakta T, Whitehead S, Snaith J, Dafforn T, Wilkie J, Rajesh S, et al. Structures of the dI2dIII1 complex of proton-translocating transhydrogenase with bound, inactive analogues of NADH and NADPH reveal active site geometries. Biochemistry. 2007;46:3304-18 pubmed
    ..Molecular dynamics simulations of the enzyme indicate that the (dihydro)nicotinamide rings remain close to a ground state for hydride transfer throughout a 1.4 ns trajectory. ..
  31. Dey S, North J, Sriram J, Evans B, Tabita F. In Vivo Studies in Rhodospirillum rubrum Indicate That Ribulose-1,5-bisphosphate Carboxylase/Oxygenase (Rubisco) Catalyzes Two Obligatorily Required and Physiologically Significant Reactions for Distinct Carbon and Sulfur Metabolic Pathways. J Biol Chem. 2015;290:30658-68 pubmed publisher
    ..Thus, despite the coevolution of both functions, the active site of this protein may be differentially modified to affect only one of its key functions. ..
  32. Schneider G, Lindqvist Y, Branden C, Lorimer G. Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9 A resolution. EMBO J. 1986;5:3409-15 pubmed
    ..There are also interactions between the N-terminal domain of one subunit and the C-terminal domain of the second subunit, close to the active site. ..
  33. Salemme F, Freer S, Alden R, Kraut J. Atomic coordinates for ferricytochrome c2 of Rhodospirillum rubrum. Biochem Biophys Res Commun. 1973;54:47-52 pubmed
  34. Falcone D, Tabita F. Complementation analysis and regulation of CO2 fixation gene expression in a ribulose 1,5-bisphosphate carboxylase-oxygenase deletion strain of Rhodospirillum rubrum. J Bacteriol. 1993;175:5066-77 pubmed
    ..The placement and orientation of the cbbR transcriptional regulator gene in R. rubrum are unique...
  35. Kerby R, Hong S, Ensign S, Coppoc L, Ludden P, Roberts G. Genetic and physiological characterization of the Rhodospirillum rubrum carbon monoxide dehydrogenase system. J Bacteriol. 1992;174:5284-94 pubmed
    ..From mutant characterizations, we posit that cooH and cooFS are not cotranscribed. The second partial ORF starts 67 bp downstream of cooS and would be capable of encoding 35 amino acids with an ATP-binding site motif...
  36. Lundqvist T, Schneider G. Crystal structure of the ternary complex of ribulose-1,5-bisphosphate carboxylase, Mg(II), and activator CO2 at 2.3-A resolution. Biochemistry. 1991;30:904-8 pubmed
    ..Nevertheless, it is obvious that the hydrogen-bonding pattern in the vicinity of the activator site is completely altered...
  37. Zhang Y, Pohlmann E, Conrad M, Roberts G. The poor growth of Rhodospirillum rubrum mutants lacking PII proteins is due to an excess of glutamine synthetase activity. Mol Microbiol. 2006;61:497-510 pubmed publisher
    ..rubrum mutants lacking P(II) and presumably in mutants of some other organisms with similar genotypes. The result underscores the importance of proper regulation of GS activity for cell growth...
  38. Cohen I, Sapir Y, Shapira M. A conserved mechanism controls translation of Rubisco large subunit in different photosynthetic organisms. Plant Physiol. 2006;141:1089-97 pubmed publisher
    ..In the case that regulation of type I and type II Rubisco is conserved, the SSU does not appear to be directly involved in LSU translation...
  39. Lundqvist T, Schneider G. Crystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate. J Biol Chem. 1991;266:12604-11 pubmed
    ..There are, however, some significant differences at the active site, especially in the metal coordination sphere...
  40. Brunisholz R, Suter F, Zuber H. The light-harvesting polypeptides of Rhodospirillum rubrum. I. The amino-acid sequence of the second light-harvestng polypeptide B 880-beta (B 870-beta) of Rhodospirillum rubrum S 1 and the carotenoidless mutant G-9+. carotenoidless mutant G-9+. Hoppe Seylers Z Physiol Chem. 1984;365:675-88 pubmed
    ..Based on the primary structure data a possible arrangement of both light-harvesting polypeptides within the membrane will be discussed...
  41. Edgren T, Nordlund S. The fixABCX genes in Rhodospirillum rubrum encode a putative membrane complex participating in electron transfer to nitrogenase. J Bacteriol. 2004;186:2052-60 pubmed
    ..rubrum. Furthermore, we suggest that FixC is the link between nitrogen fixation and the proton motive force generated in the photosynthetic reactions...
  42. Loveless T, Bishop P. Identification of genes unique to Mo-independent nitrogenase systems in diverse diazotrophs. Can J Microbiol. 1999;45:312-7 pubmed
    ..gestii possess the potential to express the Fe-only nitrogenase (nitrogenase 3). Like Azotobacter vinelandii, Azotobacter paspali appears to have the potential to express both the V-containing nitrogenase and the Fe-only nitrogenase...
  43. Ferry J. CO dehydrogenase. Annu Rev Microbiol. 1995;49:305-33 pubmed publisher
    ..These microbes obtain energy for growth via a respiratory pathway in which the methyl and carbonyl groups are oxidized to CO2, and sulfate is reduced to sulfide...
  44. Fox J, Kerby R, Roberts G, Ludden P. Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme. J Bacteriol. 1996;178:1515-24 pubmed
    ..CooH lacks the C-terminal peptide that is found in other Ni-Fe hydrogenases; in other systems, this peptide is cleaved during Ni processing...
  45. Prasad G, Wahlberg M, Sridhar V, Sundaresan V, Yamaguchi M, Hatefi Y, et al. Crystal structures of transhydrogenase domain I with and without bound NADH. Biochemistry. 2002;41:12745-54 pubmed
    ..e., oxidation state, of the nicotinamides. The comparisons illustrate how nicotinamide oxidation state can affect the domain I conformation, which is relevant to the hydride transfer step of the overall reaction...
  46. Fox J, He Y, Shelver D, Roberts G, Ludden P. Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum. J Bacteriol. 1996;178:6200-8 pubmed
    ..We also show that expression of the cooMKLXUH operon is regulated by CO and the transcriptional activator CooA in a manner similar to that of the cooFSCTJ operon that encodes the subunits of CODH and related proteins...
  47. Addlesee H, Hunter C. Rhodospirillum rubrum possesses a variant of the bchP gene, encoding geranylgeranyl-bacteriopheophytin reductase. J Bacteriol. 2002;184:1578-86 pubmed
  48. Drennan C, Heo J, Sintchak M, Schreiter E, Ludden P. Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase. Proc Natl Acad Sci U S A. 2001;98:11973-8 pubmed publisher
    ..The two Rossmann domains contribute ligands to the active site C-cluster. This x-ray structure provides insight into the mechanism of biological CO oxidation and has broader significance for the roles of Ni and Fe in biological systems...
  49. Clemente T, Shah D, Tran M, Stark D, Padgette S, Dennis D, et al. Sequence of PHA synthase gene from two strains of Rhodospirillum rubrum and in vivo substrate specificity of four PHA synthases across two heterologous expression systems. Appl Microbiol Biotechnol. 2000;53:420-9 pubmed
    ..These observations suggest that the composition of the PHA from the PHA-producing organisms does not necessarily reflect the inherent specificity of the PHA synthase...
  50. Buckley P, Baz Jackson J, Schneider T, White S, Rice D, Baker P. Protein-protein recognition, hydride transfer and proton pumping in the transhydrogenase complex. Structure. 2000;8:809-15 pubmed
    ..We propose that this movement is responsible for switching between the forbidden and allowed states for hydride transfer during proton pumping...
  51. Zhang Y, Pohlmann E, Ludden P, Roberts G. Mutagenesis and functional characterization of the glnB, glnA, and nifA genes from the photosynthetic bacterium Rhodospirillum rubrum. J Bacteriol. 2000;182:983-92 pubmed
  52. Heo J, Wolfe M, Staples C, Ludden P. Converting the NiFeS carbon monoxide dehydrogenase to a hydrogenase and a hydroxylamine reductase. J Bacteriol. 2002;184:5894-7 pubmed
    ..Both Cys(531) and His(265) are ligands to the active-site cluster of CODH. Further, CODH with Fe substituted for Ni at the active site acquires hydroxylamine reductase activity...
  53. Zou X, Zhu Y, Pohlmann E, Li J, Zhang Y, Roberts G. Identification and functional characterization of NifA variants that are independent of GlnB activation in the photosynthetic bacterium Rhodospirillum rubrum. Microbiology. 2008;154:2689-99 pubmed publisher
    ..This suggests that the necessary alteration of the pool of effector(s) for NifA activation cannot be obtained by knockout mutations...
  54. Wolfe D, Zhang Y, Roberts G. Specificity and regulation of interaction between the PII and AmtB1 proteins in Rhodospirillum rubrum. J Bacteriol. 2007;189:6861-9 pubmed publisher
    ..This supports a model where multiple 2-KG and ATP molecules must bind a P(II) trimer to stimulate release of P(II) from AmtB(1), in contrast to the lower 2-KG requirement for productive uridylylation of P(II) by GlnD...
  55. Igarashi R, Meyer C. Cloning and sequencing of glycogen metabolism genes from Rhodobacter sphaeroides 2.4.1. Expression and characterization of recombinant ADP-glucose pyrophosphorylase. Arch Biochem Biophys. 2000;376:47-58 pubmed publisher
    ..The recombinant enzyme was purified to near homogeneity and found to be physically, immunologically, and kinetically identical to the native enzyme, verifying the fidelity of the cloning step...
  56. Baltscheffsky M, Nadanaciva S, Schultz A. A pyrophosphate synthase gene: molecular cloning and sequencing of the cDNA encoding the inorganic pyrophosphate synthase from Rhodospirillum rubrum. Biochim Biophys Acta. 1998;1364:301-6 pubmed
    ..The deduced protein contains 660 amino acid residues and 15 putative membrane-spanning segments. It is homologous to the vacuolar pyrophosphatases from plants...
  57. Fitzmaurice W, Saari L, Lowery R, Ludden P, Roberts G. Genes coding for the reversible ADP-ribosylation system of dinitrogenase reductase from Rhodospirillum rubrum. Mol Gen Genet. 1989;218:340-7 pubmed
    ..rubrum is the first in which both the target protein and modifying enzymes as well as their structural genes have been isolated, making it the model system of choice for analysis of this post-translational regulatory mechanism...
  58. Kerby R, Ludden P, Roberts G. In vivo nickel insertion into the carbon monoxide dehydrogenase of Rhodospirillum rubrum: molecular and physiological characterization of cooCTJ. J Bacteriol. 1997;179:2259-66 pubmed
  59. Salemme F, Freer S, Xuong N, Alden R, Kraut J. The structure of oxidized cytochrome c 2 of Rhodospirillum rubrum. J Biol Chem. 1973;248:3910-21 pubmed
  60. Lanzilotta W, Schuller D, Thorsteinsson M, Kerby R, Roberts G, Poulos T. Structure of the CO sensing transcription activator CooA. Nat Struct Biol. 2000;7:876-80 pubmed publisher
  61. L pez Marqu s R, P rez Casti eira J, Losada M, Serrano A. Differential regulation of soluble and membrane-bound inorganic pyrophosphatases in the photosynthetic bacterium Rhodospirillum rubrum provides insights into pyrophosphate-based stress bioenergetics. J Bacteriol. 2004;186:5418-26 pubmed publisher
    ..These results demonstrate a tight transcriptional regulation of the H(+)-PPase gene, which appears to be induced in response to a variety of environmental conditions, all of which constrain cell energetics...
  62. Cotton N, White S, Peake S, McSweeney S, Jackson J. The crystal structure of an asymmetric complex of the two nucleotide binding components of proton-translocating transhydrogenase. Structure. 2001;9:165-76 pubmed
    ..The asymmetry of the dI:dIII complex suggests that in the intact enzyme there is an alternation of conformation at the catalytic sites associated with changes in nucleotide binding during proton translocation...
  63. Shelver D, Kerby R, He Y, Roberts G. Carbon monoxide-induced activation of gene expression in Rhodospirillum rubrum requires the product of cooA, a member of the cyclic AMP receptor protein family of transcriptional regulators. J Bacteriol. 1995;177:2157-63 pubmed
    ..Adjacent to cooA are two genes, nadB and nadC, with predicted products similar to proteins in other bacteria that catalyze reactions in the de novo synthesis of NAD.(ABSTRACT TRUNCATED AT 250 WORDS)..
  64. Kerby R, Youn H, Roberts G. RcoM: a new single-component transcriptional regulator of CO metabolism in bacteria. J Bacteriol. 2008;190:3336-43 pubmed publisher
    ..The genetic linkage of rcoM with both aerobic (cox) and anaerobic (coo) CO oxidation systems suggests that in different organisms RcoM proteins may control either regulon type...