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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
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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
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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
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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
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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
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