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Results: 71
Number of items: 71
  • Open Access
    Albracht, S. P. J., Meijer, A. J., & Rydström, J. (2011). Mammalian NADH:ubiquinone oxidoreductase (Complex I) and nicotinamide nucleotide transhydrogenase (Nnt) together regulate the mitochondrial production of H₂O₂--implications for their role in disease, especially cancer. Journal of Bioenergetics and Biomembranes, 43(5), 541-564. https://doi.org/10.1007/s10863-011-9381-4
  • Albracht, S. P. J. (2010). The reaction of NADPH with bovine mitochondrial NADH:ubiquinone oxidoreductase revisited: II. Comparison of the proposed working hypothesis with literature data. Journal of Bioenergetics and Biomembranes, 42(4), 279-292. https://doi.org/10.1007/s10863-010-9302-y
  • Open Access
    Albracht, S. P. J. (2010). The reaction of NADPH with bovine mitochondrial NADH:ubiquinone oxidoreductase revisited: I. Proposed consequences for electron transfer in the enzyme. Journal of Bioenergetics and Biomembranes, 42(4), 261-278. https://doi.org/10.1007/s10863-010-9301-z
  • Silakov, A., Wenk, B., Reijerse, E., Albracht, S. P. J., & Lubitz, W. (2009). Spin distribution of the H-cluster in the H(ox)-CO state of the [FeFe] hydrogenase from Desulfovibrio desulfuricans: HYSCORE and ENDOR study of (14)N and (13)C nuclear interactions. Journal of Biological Inorganic Chemistry, 14(2), 301-313. https://doi.org/10.1007/s00775-008-0449-5
  • Hoeben, F. J. M., Meijer, F. S., Dekker, C., Albracht, S. P. J., Heering, H. A., & Lemay, S. G. (2008). Toward single-enzyme molecule electrochemistry: [NiFe]-hydrogenase protein film voltammetry at nanoelectrodes. ACS Nano, 2(12), 2497-2504. https://doi.org/10.1021/nn800518d
  • Hoeben, F. J. M., Heller, I., Albracht, S. P. J., Dekker, C., Lemay, S. G., & Heering, H. A. (2008). Polymyxin-coated Au and carbon nanotube electrodes for stable [NiFe]-hydrogenase film voltammetry. Langmuir, 24(11), 5925-5931. https://doi.org/10.1021/la703984z
  • Silakov, A., Reijerse, E. J., Albracht, S. P. J., Hatchikian, E. C., & Lubitz, W. (2007). The electronic structure of the H-cluster in the [FeFe]-hydrogenase from Desulfovibrio desulfuricans: a Q-band 57Fe-ENDOR and HYSCORE study. Journal of the American Chemical Society, 129(37), 11447-11458. https://doi.org/10.1021/ja072592s
  • Schroder, O., Bleijlevens, B., de Jongh, T. E., Chen, Z., Li, T., Fischer, J., Forster, J., Friedrich, C. G., Bagley, K. A., Albracht, S. P. J., & Lubitz, W. (2007). Characterization of a cyanobacterial-like uptake [NiFe] hydrogenase: EPR and FTIR spectroscopic studies of the enzyme from Acidithiobacillus ferrooxidans. Journal of Biological Inorganic Chemistry, 12(2), 212-233. https://doi.org/10.1007/s00775-006-0185-7
  • Long, M., Liu, J., Chen, Z., Bleijlevens, B., Roseboom, W., & Albracht, S. P. J. (2007). Characterization of a HoxEFUYH type of [NiFe] hydrogenase from Allochromatium vinosum and some EPR and IR properties of the hydrogenase module. Journal of Biological Inorganic Chemistry, 12(1), 62-78. https://doi.org/10.1007/s00775-006-0162-1
  • Albracht, S. P. J., Roseboom, W., & Hatchikian, E. C. (2006). The active site of the [FeFe]-hydrogenase from D. desulfuricans. I: Light sensitivity and magnetic hyperfine interactions as observed by electron paramagnetic resonance. Journal of Biological Inorganic Chemistry, 11, 88-101. https://doi.org/10.1007/s00775-005-0039-8
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