Reference : Monitoring the zinc affinity of the metallo-beta-lactamase CphA by automated nanoESI-MS
Scientific journals : Article
Physical, chemical, mathematical & earth Sciences : Physics
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/9380
Monitoring the zinc affinity of the metallo-beta-lactamase CphA by automated nanoESI-MS
English
De Vriendt, K. [> > > >]
Van Driessche, G. [> > > >]
Devreese, B. [> > > >]
Bebrone, Carine mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Anne, C. [> > > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > Département des sciences de la vie > Département des sciences de la vie >]
Galleni, Moreno mailto [Université de Liège - ULg > Département des sciences de la vie > Macromolécules biologiques >]
Van Beeumen, Jos [> > > >]
Feb-2006
Journal of the American Society for Mass Spectrometry
Elsevier Science Inc
17
2
180-188
Yes (verified by ORBi)
International
1044-0305
New York
[en] Metallo-beta-lactamases are zinc containing enzymes that are able to hydrolyze and inactivate beta-lactam antibiotics. The subclass B2 enzyme CphA of Aeromonas hydrophila is a unique metallo-p-lactamase because it degrades only carbapenems efficiently and is only active when it has one zinc ion bound. A zinc titration experiment was used to study the zinc affinity of the wild-type and of several mutant CphA enzymes. It shows that a second Zn2+ is also bound at high ion concentrations. All samples were analyzed using mass spectrometry in combination with an automated nanoESI source. The metal-free enzyme has a bimodal charge distribution indicative of two conformational states. A completely folded enzyme is detected when the apo-enzyme has bound the first zinc. Intensity ratios of the different enzyme forms were used to deduce the zinc affinities. CphA enzymes mutated in metal ligands show decreased zinc affinity compared to wild-type, especially D120 mutants.
http://hdl.handle.net/2268/9380
http://www.elsevier.com/wps/find/journaldescription.cws_home/505727/description#description
The authors acknowledge the Journal of American Society for Mass Spectrometry and Elsevier.

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