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Results: 6,128
Number of items: 6,128
  • Buist, A. H., Müller, M., Ghauharali, R. I., Brakenhoff, G. J., Squier, J., Bardeen, C. J., Yakovlev, V. V., & Wilson, K. R. (1999). Probing microscopic chemical environments with high intensity chirped pulses. Optics Letters, 24(4), 244-246. https://doi.org/10.1364/OL.24.000244
  • Wever, R., & Hemrika, W. (1999). Vanadium in enzymes. In J. O. Nriagu (Ed.), Vanadium in the environment, part I (pp. 285-305). John Wiley & Sons.
  • Averill, B. A., Tramper, J., Laane, N. W. M., & Straathof, A. (1999). Biocatalysis, Chapter 7. In P. W. N. M. van Leeuwen, R. A. van Santen, J. A. Moulijn, & B. A. Averill (Eds.), Catalysis: An integrated approach, 2nd rev. Elsevier Press.
  • Bakker, B. M., Michels, P. A. M., Opperdoes, F. R., & Westerhoff, H. V. (1999). What controls glycolysis in bloodstream form Trypanosoma brucei. The Journal of Biological Chemistry, 274, 14551-14559. https://doi.org/10.1074/jbc.274.21.14551
  • Merkx, M., Pinkse, M. W. H., & Averill, B. A. (1999). Evidence for non-bridged coordination of p-nitrophenylphosphat to the dinuclear Fe(III)-M(II) center in bovine spleen purple acid phosphatase during enzymatic turnover. Biochemistry, 38, 9914-9925. https://doi.org/10.1021/bi9904454
  • Bouritius, H., Bajnath, R. B., & Groot, J. A. (1999). Microelectrode measurements of the effects of basolateral adenosine in polarized human intestinal epithelial cells in culture. Plügers Archiv, 437, 589-595. https://doi.org/10.1007/s004240050821
  • Pershad, H. R., Duff, J. L. C., Heering, H. A., Duin, E. C., Albracht, S. P. J., & Armstrong, F. A. (1999). Catalytic electron transport in Chromatium vinosum [NiFe]-hydrogenase: appliaction of voltammetry in detecting redox-active centers and establishing that hydrogen oxidation is very fast even at potentials close to the reversible H+/H2 value. Biochemistry, 38, 8992-8999. https://doi.org/10.1021/bi990108v
  • 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
  • Pinkse, M. W. H., Merkx, M., & Averill, B. A. (1999). Fluoride inhibition of bovine spleen purple acid phosphatase: characterizatino of a ternary enzyme-phosphate-fluoride complex as a model for the active enzyme-substrate-hydroxide complex. Biochemistry, 38, 9926-9936. https://doi.org/10.1021/bi990446w
  • ten Brink, H. B., Holland, H. L., Schoemaker, H. E., van Lingen, H., & Wever, R. (1999). Probing the scope of the sulfoxidation activity of vanadium bromoperoxidase from Ascophyllum nodosum. Tetrahedron-Asymmetry, 10, 4563-4572. https://doi.org/10.1016/S0957-4166(99)00514-5
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