Year |
Citation |
Score |
2017 |
Mitić S, Strampraad MJF, Hagen WR, de Vries S. Microsecond time-scale kinetics of transient biochemical reactions. Plos One. 12: e0185888. PMID 28973014 DOI: 10.1371/journal.pone.0185888 |
0.477 |
|
2016 |
Gnandt E, Dörner K, Strampraad MF, de Vries S, Friedrich T. The multitude of iron-sulfur clusters in respiratory complex I. Biochimica Et Biophysica Acta. PMID 26944855 DOI: 10.1016/j.bbabio.2016.02.018 |
0.322 |
|
2015 |
Paulus A, Werner C, Ludwig B, de Vries S. The cytochrome ba3 oxidase from Thermus thermophilus does not generate a tryptophan radical during turnover: Implications for the mechanism of proton pumping. Biochimica Et Biophysica Acta. PMID 26009016 DOI: 10.1016/j.bbabio.2015.05.013 |
0.32 |
|
2005 |
Hagedoorn PL, Chen T, Schröder I, Piersma SR, de Vries S, Hagen WR. Purification and characterization of the tungsten enzyme aldehyde:ferredoxin oxidoreductase from the hyperthermophilic denitrifier Pyrobaculum aerophilum. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 10: 259-69. PMID 15772818 DOI: 10.1007/s00775-005-0637-5 |
0.541 |
|
2004 |
Suharti, Heering HA, de Vries S. NO reductase from Bacillus azotoformans is a bifunctional enzyme accepting electrons from menaquinol and a specific endogenous membrane-bound cytochrome c551. Biochemistry. 43: 13487-95. PMID 15491156 DOI: 10.1021/bi0488101 |
0.382 |
|
2004 |
Heering HA, Wiertz FG, Dekker C, de Vries S. Direct immobilization of native yeast iso-1 cytochrome C on bare gold: fast electron relay to redox enzymes and zeptomole protein-film voltammetry. Journal of the American Chemical Society. 126: 11103-12. PMID 15339197 DOI: 10.1021/Ja046737W |
0.305 |
|
2001 |
Afshar S, Johnson E, de Vries S, Schröder I. Properties of a thermostable nitrate reductase from the hyperthermophilic archaeon Pyrobaculum aerophilum. Journal of Bacteriology. 183: 5491-5. PMID 11544209 DOI: 10.1128/Jb.183.19.5491-5495.2001 |
0.319 |
|
2001 |
Suharti, Strampraad MJ, Schröder I, de Vries S. A novel copper A containing menaquinol NO reductase from Bacillus azotoformans. Biochemistry. 40: 2632-9. PMID 11327887 DOI: 10.1021/bi0020067 |
0.307 |
|
2000 |
De Jong GAH, Tang JA, Bos P, De Vries S, Kuenen JG. Purification and characterization of a sulfite: Cytochrome c oxidoreductase from Thiobacillus acidophilus Journal of Molecular Catalysis - B Enzymatic. 8: 61-67. DOI: 10.1016/S1381-1177(99)00067-3 |
0.308 |
|
1997 |
Girsch P, De Vries S. Purification and initial kinetic and spectroscopic characterization of NO reductase from Paracoccus denitrificans Biochimica Et Biophysica Acta - Bioenergetics. 1318: 202-216. PMID 9030265 DOI: 10.1016/S0005-2728(96)00138-7 |
0.337 |
|
1991 |
Marres CAM, de Vries S. Reduction of the Q-pool by duroquinol via the two quinone-binding sites of the QH2: cytochrome c oxidoreductase. A model for the equilibrium between cytochrome b-562 and the Q-pool Bba - Bioenergetics. 1057: 51-63. PMID 1849003 DOI: 10.1016/S0005-2728(05)80083-0 |
0.335 |
|
1987 |
van Hoek AN, van Gaalen MC, de Vries S, Berden JA. 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. Biochimica Et Biophysica Acta. 892: 152-61. PMID 3034326 DOI: 10.1016/0005-2728(87)90257-X |
0.332 |
|
1983 |
De Vries S, Albracht SP, Berden JA, Marres CA, Slater EC. The effect of pH, ubiquinone depletion and myxothiazol on the reduction kinetics of the prosthetic groups of ubiquinol:cytochrome c oxidoreductase. Biochimica Et Biophysica Acta. 723: 91-103. PMID 6299337 DOI: 10.1016/0005-2728(83)90013-0 |
0.661 |
|
1982 |
Zhu QS, Berden JA, De Vries S, Slater EC. On the role of ubiquinone in the respiratory chain. Biochimica Et Biophysica Acta. 680: 69-79. PMID 7074101 DOI: 10.1016/0005-2728(82)90317-6 |
0.551 |
|
1982 |
Zhu QS, Berden JA, De Vries S, Folkers K, Porter T, Slater EC. Identification of two different Q-binding sites in QH2-cytochrome c oxidoreductase, using the Q analogue n-heptadecylmercapto-6-hydroxy-5,8-quinolinequinone. Biochimica Et Biophysica Acta. 682: 160-7. PMID 6291602 DOI: 10.1016/0005-2728(82)90130-X |
0.572 |
|
1982 |
Marres CA, De Vries S, Slater EC. The site of inhibition by 5,5'-dithiobis(2-nitrobenzoate) in ubiquinol: cytochrome c oxidoreductase. Biochimica Et Biophysica Acta. 681: 323-6. PMID 6288087 DOI: 10.1016/0005-2728(82)90039-1 |
0.601 |
|
1982 |
De Vries S, Albracht SP, Berden JA, Slater EC. The pathway of electrons through OH2:cytochrome c oxidoreductase studied by pre-steady -state kinetics. Biochimica Et Biophysica Acta. 681: 41-53. PMID 6288082 DOI: 10.1016/0005-2728(82)90276-6 |
0.673 |
|
1981 |
de Vries S, Albracht SP, Berden JA, Slater EC. A new species of bound ubisemiquinone anion in QH2: cytochrome c oxidoreductase. The Journal of Biological Chemistry. 256: 11996-8. PMID 6271770 |
0.626 |
|
1980 |
de Vries S, Berden JA, Slater EC. Properties of a semiquinone anion located in the QH2:cytochrome c oxidoreductase segment of the mitochondrial respiratory chain. Febs Letters. 122: 143-8. PMID 7215541 DOI: 10.1016/0014-5793(80)80422-4 |
0.466 |
|
1980 |
Slater EC, de Vries S. Identification of the BAL-labile factor. Nature. 288: 717-8. PMID 6256640 DOI: 10.1038/288717a0 |
0.56 |
|
1979 |
de Vries S, Albracht SP. Intensity of highly anisotropic low-spin heme EPR signals. Biochimica Et Biophysica Acta. 546: 334-40. PMID 221015 DOI: 10.1016/0005-2728(79)90050-1 |
0.463 |
|
1979 |
de Vries S, Albracht SP, Leeuwerik FJ. The multiplicity and stoichiometry of the prosthetic groups in QH2: cytochrome c oxidoreductase as studied by EPR. Biochimica Et Biophysica Acta. 546: 316-33. PMID 221014 DOI: 10.1016/0005-2728(79)90049-5 |
0.61 |
|
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