Search results

  • Full text

  • Document type

    • Publication year

  • Organisation

Results: 41
Number of items: 41
  • 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
  • Roseboom, W., De Lacey, A. L., Fernandez, V. M., Hatchikian, E. C., & Albracht, S. P. J. (2006). The active site of the [FeFe]-hydrogenase from D. desulfuricans. II: Redox properties, light sensitivity and CO-ligand exchange as observed by infrared spectroscopy. Journal of Biological Inorganic Chemistry, 11, 102-118. https://doi.org/10.1007/s00775-005-0040-2
  • Bleijlevens, B., van Broekhuizen, F. A., De Lacey, A. L., Roseboom, W., Fernandez, V. M., & Albracht, S. P. J. (2004). The activation of the [NiFe]-hydrogenase from Allochromatium vinosum. An infrared spectro-electrochemical study. Journal of Biological Inorganic Chemistry, 9, 743-752. https://doi.org/10.1007/s00775-004-0570-z
  • Lyon, E. J., Shima, S., Boecher, R., Thauer, R. K., Grevels, F.-W., Bill, E., Roseboom, W., & Albracht, S. P. J. (2004). Carbon monoxide as an intrinsic ligand to iron in the active site of te iron-sulfur-cluster-free hydrogenase H(2)-forming methylenetetrahydromethanopterin dehydrogenase as revealed by infrared spectroscopy. Journal of the American Chemical Society, 126, 14239-14248. https://doi.org/10.1021/ja046818s
  • Happe, R. P., Roseboom, W., Egert, G., Friedrich, C. G., Massanz, C., Friedrich, B., & Albracht, S. P. J. (2000). Unusual FTIR and EPR properties of the H2-activating site of the cytoplasmic NAD-reducing hydrogenase from Ralstonia eutropha. FEBS Letters, 466, 259-263. https://doi.org/10.1016/S0014-5793(99)01799-8
  • Davidson, G., Choudhury, S. B., Gu, Z., Bose, K., Roseboom, W., Albracht, S. P. J., & Maroney, M. J. (2000). Structural examination of the nickel site in Chromatium vinosum hydrogenase: redox state oscillations and structural changes accompanying reductive activation and CO binding. Biochemistry, 39, 7468-7479. https://doi.org/10.1021/bi000300t
  • Pierik, A. J., Roseboom, W., Happe, R. P., Bagley, K. A., & Albracht, S. P. J. (1999). Carbon monoxide and cyanide as intrinsic ligands to iron in the active site of [NiFe}-hydrogenases. NiFe(CN)2CO, biology's way to activate H2. The Journal of Biological Chemistry, 274, 3331-3337. https://doi.org/10.1074/jbc.274.6.3331
  • 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.
  • 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
Page 4 of 5