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.
%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
}