%0 Journal Article %1 hernandez_valladares_kinetic_2000 %A Valladares, Maria Hernandez %A Kiefer, Martin %A Heinz, Uwe %A Soto, Raquel Paul %A Meyer-Klaucke, Wolfram %A Nolting, Hans Friederich %A Zeppezauer, Michael %A Galleni, Moreno %A Frère, Jean-Marie %A Rossolini, Gian Maria %A Amicosante, Gianfranco %A Adolph, Hans-Werner %D 2000 %J FEBS Letters %K Kinetics, Metal Metallo-[beta]-lactamase, exchange, spectroscopy {EXAFS,} {UV-vis} %N 2-3 %P 221--225 %R 10.1016/S0014-5793(00)01102-9 %T Kinetic and spectroscopic characterization of native and metal-substituted beta-lactamase from Aeromonas hydrophila AE036 %U http://www.sciencedirect.com/science/article/B6T36-3YHFGS6-M/2/e3dd2af2c3ecc3ec298814914c592d77 %V 467 %X Two metal ion binding sites are conserved in metallo-beta-lactamase from Aeromonas hydrophila. The ligands of a first zinc ion bound with picomolar dissociation constant were identified by EXAFS spectroscopy as one Cys, two His and one additional N/O donor. Sulfur-to-metal charge transfer bands are observed for all mono- and di-metal species substituted with Cu(II) or Co(II) due to ligation of the single conserved cysteine residue. Binding of a second metal ion results in non-competitive inhibition which might be explained by an alternative kinetic mechanism. A possible partition of metal ions between the two binding sites is discussed.

@article{hernandez_valladares_kinetic_2000, abstract = {Two metal ion binding sites are conserved in metallo-[beta]-lactamase from Aeromonas hydrophila. The ligands of a first zinc ion bound with picomolar dissociation constant were identified by {EXAFS} spectroscopy as one Cys, two His and one additional {N/O} donor. Sulfur-to-metal charge transfer bands are observed for all mono- and di-metal species substituted with {Cu(II)} or {Co(II)} due to ligation of the single conserved cysteine residue. Binding of a second metal ion results in non-competitive inhibition which might be explained by an alternative kinetic mechanism. A possible partition of metal ions between the two binding sites is discussed.}, added-at = {2011-03-11T10:05:34.000+0100}, author = {Valladares, Maria Hernandez and Kiefer, Martin and Heinz, Uwe and Soto, Raquel Paul and {Meyer-Klaucke}, Wolfram and Nolting, Hans Friederich and Zeppezauer, Michael and Galleni, Moreno and Frère, {Jean-Marie} and Rossolini, Gian Maria and Amicosante, Gianfranco and Adolph, {Hans-Werner}}, biburl = {https://www.bibsonomy.org/bibtex/22d1b6a3e3deda2b7efc1ac320b8dd7c6/jelias}, doi = {10.1016/S0014-5793(00)01102-9}, interhash = {e381b127a35767948edf7957812da04c}, intrahash = {2d1b6a3e3deda2b7efc1ac320b8dd7c6}, issn = {0014-5793}, journal = {{FEBS} Letters}, keywords = {Kinetics, Metal Metallo-[beta]-lactamase, exchange, spectroscopy {EXAFS,} {UV-vis}}, month = feb, number = {2-3}, pages = {221--225}, timestamp = {2011-03-11T10:06:33.000+0100}, title = {Kinetic and spectroscopic characterization of native and metal-substituted [beta]-lactamase from Aeromonas hydrophila {AE036}}, url = {http://www.sciencedirect.com/science/article/B6T36-3YHFGS6-M/2/e3dd2af2c3ecc3ec298814914c592d77}, volume = 467, year = 2000 }