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Results: 71
Number of items: 71
  • Geßner, C., Stein, M., Albracht, S. P. J., & Lubits, W. (1999). Orientation-selected ENDOR of the active center in Chromatium vinosum [NiFe]-hydrogenase in the oxidized, 'ready' state. Journal of Biological Inorganic Chemistry, 4(4), 379-389. https://doi.org/10.1007/s007750050324
  • Happe, R. P., Roseboom, W., & Albracht, S. P. J. (1999). Pre-steady-state kinetics of the reactions of [NiFe]-hydrogenase from Chromatium vinosum with H2 and CO. European Journal of Biochemistry, 259, 602-609. https://doi.org/10.1046/j.1432-1327.1999.00057.x
  • Happe, R. P., Roseboom, W., Pierik, A. J., Albracht, S. P. J., & Bagley, K. A. (1997). Biological activation of hydrogen. Nature, (385), 126-126.
  • Albracht, S. P. J., & de Jong, A. M. P. (1997). Hypothesis: Bovine-heart NADH: ubiquinone oxidoreductase is a monomer with 8 Fe-S clusters and 2 FMN groups. Biochimica et Biophysica Acta, (1318), 92-106.
  • Open Access
    van Belzen, R., Kotlyar, A. B., Moon, N., Dunham, W. R., & Albracht, S. P. J. (1997). The iron-sulfur clusters 2 and ubisemiquinone radicals of NADH: ubiquinone oxidoreductase are involved in energy coupling in submitochondrial particles. Biochemistry, (36), 886-893.
  • Open Access
    Chevallet, M., Dupuis, A., Lunardi, J., van Belzen, R., Albracht, S. P. J., & Issartel, J. P. (1997). The NUOI subunit of the Rhodobacter capsulatus respiratory Complex I (equivalent to the bovine TYKY subunit) is required for proper assembly of the membraneous and peripheral domains of the enzyme. European Journal of Biochemistry, (250), 451-458.
  • Open Access
    Sorgenfrei, O., Duin, E. C., de Klein, A., & Albracht, S. P. J. (1997). Changes in the electronic structure around Ni in oxidized and reduced selenium-containing hydrogenases from Methanococcus voltae. European Journal of Biochemistry, (247), 681-687.
  • Open Access
    Boll, M., Albracht, S. P. J., & Fuchs, G. (1997). Benzoyl-CoA reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. Study of adenosinetriphosphatase activity, ATP stoichiometry of the reaction and EPR properties of the enzyme. European Journal of Biochemistry, (244), 840-851.
  • Open Access
    Speijer, D., Breek, C. K. D., Muijsers, A. O., Hartog, A. F., Berden, J. A., Albracht, S. P. J., Samyn, B., Van Beeumen, J., & Benne, R. (1997). Characterization of the respiratory chain from cultured Crithidia fasciculata. Molecular and biochemical parasitology, 85(2), 171-186. https://doi.org/10.1016/S0166-6851(96)02823-X
  • Gu, Z., Dong, J., Allan, C. B., Choudhury, S. B., Franco, R., Moura, J. J. G., Moura, I., LeGall, J., Przybylia, A. E., Roseboom, W., Albracht, S. P. J., Axley, M. J., Scott, R. A., & Maroney, M. J. (1996). Structure of the Ni sites in hydrogenases by X-ray absorption spectroscopy. Species variation and effects of redox poise. Journal of the American Chemical Society, 118, 11155-11165. https://doi.org/10.1021/ja962429p
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