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)
 
Chemical Compound Review

duroquinol     4-hydroxy-2,3,5,6- tetramethyl-cyclohexa-2...

Synonyms: CTK8D6321, AR-1D4116, AC1L3X9G, AC1Q6A8J
 
 
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 duroquinol

 

High impact information on duroquinol

 

Biological context of duroquinol

 

Anatomical context of duroquinol

 

Associations of duroquinol with other chemical compounds

 

Gene context of duroquinol

  • C. reinhardtii and S. obliquus complexes contain the Rieske iron-sulfur protein (present in approx 1:1 molar ratio to cytochrome f) and each catalyzes a DBMIB- and DNP-INT-sensitive electron transfer from duroquinol to spinach plastocyanin [19].
  • Under such circumstances, the addition of a limited amount of either succinate or duroquinol leads to a multiphasic reduction and oxidation of cytochrome b [20].
  • Assays of partial electron transport activities indicate a site of inhibition in the region between the site of duroquinol oxidation and cytochrome c reduction [21].
  • Finally, the addition of the type 2 NADH:quinone oxidoreductase complex (NADH dehydrogenase [NDH]) from M. capsulatus Bath, along with NADH and duroquinol, to enzyme assays increased the activity of purified preparations [15].
  • Duroquinol was a suitable reducing agent, and pMMO was stabilized by bovine serum albumin (BSA) [22].
 

Analytical, diagnostic and therapeutic context of duroquinol

References

  1. Kinetics of membrane-bound nitrate reductase A from Escherichia coli with analogues of physiological electron donors--different reaction sites for menadiol and duroquinol. Giordani, R., Buc, J., Cornish-Bowden, A., Cárdenas, M.L. Eur. J. Biochem. (1997) [Pubmed]
  2. Delineation of the catalytic components of the NADPH-dependent O2- generating oxidoreductase of human neutrophils. Green, T.R., Wirtz, M.K., Wu, D.E. Biochem. Biophys. Res. Commun. (1983) [Pubmed]
  3. Toxicity of bile acids on the electron transport chain of isolated rat liver mitochondria. Krähenbühl, S., Talos, C., Fischer, S., Reichen, J. Hepatology (1994) [Pubmed]
  4. Regulation of the uncoupling protein in brown adipose tissue. LaNoue, K.F., Strzelecki, T., Strzelecka, D., Koch, C. J. Biol. Chem. (1986) [Pubmed]
  5. The effect of glucagon on hepatic respiratory capacity. LaNoue, K.F., Strzelecki, T., Finch, F. J. Biol. Chem. (1984) [Pubmed]
  6. Isolation and properties of cytochrome b561 from bovine adrenal chromaffin granules. Duong, L.T., Fleming, P.J. J. Biol. Chem. (1982) [Pubmed]
  7. Toward delineating the structure and function of the particulate methane monooxygenase from methanotrophic bacteria. Chan, S.I., Chen, K.H., Yu, S.S., Chen, C.L., Kuo, S.S. Biochemistry (2004) [Pubmed]
  8. Aging decreases electron transport complex III activity in heart interfibrillar mitochondria by alteration of the cytochrome c binding site. Lesnefsky, E.J., Gudz, T.I., Moghaddas, S., Migita, C.T., Ikeda-Saito, M., Turkaly, P.J., Hoppel, C.L. J. Mol. Cell. Cardiol. (2001) [Pubmed]
  9. Protein PII regulates both inorganic carbon and nitrate uptake and is modified by a redox signal in synechocystis PCC 6803. Hisbergues, M., Jeanjean, R., Joset, F., Tandeau de Marsac, N., Bédu, S. FEBS Lett. (1999) [Pubmed]
  10. The effect of cold exposure on rat liver mitochondrial respiratory capacity. Liverini, G., Iossa, S., Barletta, A. Comp. Biochem. Physiol., B (1991) [Pubmed]
  11. Reversibility of hepatic mitochondrial damage in rats with long-term cholestasis. Krähenbühl, L., Schäfer, M., Krähenbühl, S. J. Hepatol. (1998) [Pubmed]
  12. Differential exposure of components of cytochrome b-c1 region in beef heart mitochondria and electron transport particles. Harmon, H.J., Basile, P.F. J. Bioenerg. Biomembr. (1982) [Pubmed]
  13. Pre-steady-state reduction kinetics of QH2:cytochrome c oxidoreductase and the Q-pool: evidence for a special quinone not in rapid equilibrium with the Q-pool. van Hoek, A.N., van Gaalen, M.C., de Vries, S., Berden, J.A. Biochim. Biophys. Acta (1987) [Pubmed]
  14. The role of cytochrome c diffusion in mitochondrial electron transport. Gupte, S.S., Hackenbrock, C.R. J. Biol. Chem. (1988) [Pubmed]
  15. The membrane-associated methane monooxygenase (pMMO) and pMMO-NADH:quinone oxidoreductase complex from Methylococcus capsulatus Bath. Choi, D.W., Kunz, R.C., Boyd, E.S., Semrau, J.D., Antholine, W.E., Han, J.I., Zahn, J.A., Boyd, J.M., de la Mora, A.M., DiSpirito, A.A. J. Bacteriol. (2003) [Pubmed]
  16. Effect of chronic hyperoxic exposure on duroquinone reduction in adult rat lungs. Audi, S.H., Bongard, R.D., Krenz, G.S., Rickaby, D.A., Haworth, S.T., Eisenhauer, J., Roerig, D.L., Merker, M.P. Am. J. Physiol. Lung Cell Mol. Physiol. (2005) [Pubmed]
  17. Evidence for two different electron transfer pathways in the same enzyme, nitrate reductase A from Escherichia coli. Giordani, R., Buc, J. Eur. J. Biochem. (2004) [Pubmed]
  18. Sites of inhibition of mitochondrial electron transport by cadmium. Miccadei, S., Floridi, A. Chem. Biol. Interact. (1993) [Pubmed]
  19. Green algal cytochrome b6-f complexes: isolation and characterization from Dunaliella saline, Chlamydomonas reinhardtii and Scenedesmus obliquus. Wynn, R.M., Bertsch, J., Bruce, B.D., Malkin, R. Biochim. Biophys. Acta (1988) [Pubmed]
  20. Multiphasic oxidation-reduction of cytochrome b in the succinate-cytochrome c reductase. Tsou, C.L., Tang, H.L., Wang, D.C., Jin, Y.Z. Biochim. Biophys. Acta (1982) [Pubmed]
  21. Inhibition of mitochondrial electron transport by hydroxy-substituted 1,4-quinones. Phelps, D.C., Crane, F.L. Biochemistry (1975) [Pubmed]
  22. Properties of the membranes containing the particulate methane monooxygenase from Methylosinus trichosporium OB3b. Takeguchi, M., Miyakawa, K., Okura, I. Biometals (1998) [Pubmed]
  23. Glucagon treatment of rats activates the respiratory chain of liver mitochondria at more than one site. Halestrap, A.P. Biochim. Biophys. Acta (1987) [Pubmed]
 
WikiGenes - Universities