The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
MeSH Review

Rhodothermus

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of Rhodothermus

  • The cytochrome c domain of subunit II from the Rhodothermus marinus caa(3) HiPIP:oxygen oxidoreductase, a member of the superfamily of heme-copper-containing terminal oxidases, was produced in Escherichia coli and characterised [1].
  • The thymidine kinase gene from the thermophilic eubacterium Rhodothermus marinus was cloned, sequenced and overexpressed [2].
 

High impact information on Rhodothermus

  • Structure at 1.3 A resolution of Rhodothermus marinus caa(3) cytochrome c domain [1].
  • Rhodothermus marinus, a thermohalophilic gram negative bacterium, contains a type I NADH/quinone oxidoreductase (complex I) [3].
  • The caa(3) terminal oxidase of Rhodothermus marinus lacking the key glutamate of the D-channel is a proton pump [4].
  • The thermohalophilic bacterium Rhodothermus marinus expresses a caa(3)-type dioxygen reductase as one of its terminal oxidases [4].
  • We demonstrate with attenuated total reflection-Fourier transform infrared (ATR-FTIR) difference spectroscopy that a tyrosine residue of the oxygen reductase from the thermohalophilic Rhodothermus marinus becomes deprotonated in the transition from the oxidized state to the catalytic intermediate ferryl state P(M) [5].
 

Chemical compound and disease context of Rhodothermus

 

Biological context of Rhodothermus

 

Gene context of Rhodothermus

 

Analytical, diagnostic and therapeutic context of Rhodothermus

  • The ppc gene, which encodes phosphoenolpyruvate carboxylase (PEPC) of an extremely thermophilic bacterium, Rhodothermus obamensis, was directly sequenced by the thermal asymmetric interlaced (TAIL) PCR method [14].

References

  1. Structure at 1.3 A resolution of Rhodothermus marinus caa(3) cytochrome c domain. Srinivasan, V., Rajendran, C., Sousa, F.L., Melo, A.M., Saraiva, L.M., Pereira, M.M., Santana, M., Teixeira, M., Michel, H. J. Mol. Biol. (2005) [Pubmed]
  2. Cloning, sequence analysis and overexpression of a rhodothermus marinus gene encoding a thermostable thymidine kinase. Blöndal, T., Thorbjarnardóttir, S.H., Kieleczawa, J., Einarsson, J.M., Hjörleifsdóttir, S., Kristjánsson, J.K., Eggertsson, G. FEMS Microbiol. Lett. (1999) [Pubmed]
  3. Electron paramagnetic resonance studies of the iron-sulfur centers from complex I of Rhodothermus marinus. Fernandes, A.S., Sousa, F.L., Teixeira, M., Pereira, M.M. Biochemistry (2006) [Pubmed]
  4. The caa(3) terminal oxidase of Rhodothermus marinus lacking the key glutamate of the D-channel is a proton pump. Pereira, M.M., Verkhovskaya, M.L., Teixeira, M., Verkhovsky, M.I. Biochemistry (2000) [Pubmed]
  5. A tyrosine residue deprotonates during oxygen reduction by the caa3 reductase from Rhodothermus marinus. Pereira, M.M., Sousa, F.L., Teixeira, M., Nyquist, R.M., Heberle, J. FEBS Lett. (2006) [Pubmed]
  6. The succinate dehydrogenase from the thermohalophilic bacterium Rhodothermus marinus: redox-Bohr effect on heme bL. Fernandes, A.S., Pereira, M.M., Teixeira, M. J. Bioenerg. Biomembr. (2001) [Pubmed]
  7. Rhodothermus marinus: a thermophilic bacterium producing dimeric and hexameric citrate synthase isoenzymes. Nordberg, K.E., Abou-Hachem, M., Holst, O., Danson, M.J., Hough, D.W. Extremophiles (2002) [Pubmed]
  8. Cloning and sequence analysis of the hemB gene of Rhodothermus marinus. Gudmundsdóttir, K., Sigurdsson, E., Thorbjarnardóttir, S.I., Eggertsson, G. Curr. Microbiol. (1999) [Pubmed]
  9. Evidence for substrate binding of a recombinant thermostable xylanase originating from Rhodothermus marinus. Karlsson, E.N., Bartonek-Roxå, E., Holst, O. FEMS Microbiol. Lett. (1998) [Pubmed]
  10. Quinone reduction by Rhodothermus marinus succinate:menaquinone oxidoreductase is not stimulated by the membrane potential. Fernandes, A.S., Konstantinov, A.A., Teixeira, M., Pereira, M.M. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  11. Cloning, expression, and characterization of a highly thermostable family 18 chitinase from Rhodothermus marinus. Hobel, C.F., Hreggvidsson, G.O., Marteinsson, V.T., Bahrani-Mougeot, F., Einarsson, J.M., Kristjánsson, J.K. Extremophiles (2005) [Pubmed]
  12. Cloning and sequence analysis of the DNA ligase-encoding gene of Rhodothermus marinus, and overproduction, purification and characterization of two thermophilic DNA ligases. Thorbjarnardóttir, S.H., Jónsson, Z.O., Andrésson, O.S., Kristjánsson, J.K., Eggertsson, G., Palsdottir, A. Gene (1995) [Pubmed]
  13. Co-operativity of hexamer ligation. Kaczorowski, T., Szybalski, W. Gene (1996) [Pubmed]
  14. ppc, the gene for phosphoenolpyruvate carboxylase from an extremely thermophilic bacterium, Rhodothermus obamensis: cloning, sequencing and overexpression in Escherichia coli. Takai, K., Sako, Y., Uchida, A. Microbiology (Reading, Engl.) (1998) [Pubmed]
 
WikiGenes - Universities