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181 related items for PubMed ID: 11551939

  • 1. Metal ion binding and coordination geometry for wild type and mutants of metallo-beta -lactamase from Bacillus cereus 569/H/9 (BcII): a combined thermodynamic, kinetic, and spectroscopic approach.
    de Seny D, Heinz U, Wommer S, Kiefer M, Meyer-Klaucke W, Galleni M, Frere JM, Bauer R, Adolph HW.
    J Biol Chem; 2001 Nov 30; 276(48):45065-78. PubMed ID: 11551939
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  • 3. Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo-beta-lactamase.
    de Seny D, Prosperi-Meys C, Bebrone C, Rossolini GM, Page MI, Noel P, Frère JM, Galleni M.
    Biochem J; 2002 May 01; 363(Pt 3):687-96. PubMed ID: 11964169
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  • 7. Coordination geometries of metal ions in d- or l-captopril-inhibited metallo-beta-lactamases.
    Heinz U, Bauer R, Wommer S, Meyer-Klaucke W, Papamichaels C, Bateson J, Adolph HW.
    J Biol Chem; 2003 Jun 06; 278(23):20659-66. PubMed ID: 12668674
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  • 9. Positively cooperative binding of zinc ions to Bacillus cereus 569/H/9 beta-lactamase II suggests that the binuclear enzyme is the only relevant form for catalysis.
    Jacquin O, Balbeur D, Damblon C, Marchot P, De Pauw E, Roberts GC, Frère JM, Matagne A.
    J Mol Biol; 2009 Oct 09; 392(5):1278-91. PubMed ID: 19665032
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  • 10. The inhibitor thiomandelic acid binds to both metal ions in metallo-beta-lactamase and induces positive cooperativity in metal binding.
    Damblon C, Jensen M, Ababou A, Barsukov I, Papamicael C, Schofield CJ, Olsen L, Bauer R, Roberts GC.
    J Biol Chem; 2003 Aug 01; 278(31):29240-51. PubMed ID: 12724330
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  • 11. Metal content and localization during turnover in B. cereus metallo-beta-lactamase.
    Llarrull LI, Tioni MF, Vila AJ.
    J Am Chem Soc; 2008 Nov 26; 130(47):15842-51. PubMed ID: 18980306
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  • 14. Engineered mononuclear variants in Bacillus cereus metallo-beta-lactamase BcII are inactive.
    Abriata LA, González LJ, Llarrull LI, Tomatis PE, Myers WK, Costello AL, Tierney DL, Vila AJ.
    Biochemistry; 2008 Aug 19; 47(33):8590-9. PubMed ID: 18652482
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  • 15. Enzyme deactivation due to metal-ion dissociation during turnover of the cobalt-beta-lactamase catalyzed hydrolysis of beta-lactams.
    Badarau A, Page MI.
    Biochemistry; 2006 Sep 12; 45(36):11012-20. PubMed ID: 16953588
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  • 16. Grafting a new metal ligand in the cocatalytic site of B. cereus metallo-beta-lactamase: structural flexibility without loss of activity.
    Rasia RM, Ceolín M, Vila AJ.
    Protein Sci; 2003 Jul 12; 12(7):1538-46. PubMed ID: 12824499
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  • 18. Exploring the role and the binding affinity of a second zinc equivalent in B. cereus metallo-beta-lactamase.
    Rasia RM, Vila AJ.
    Biochemistry; 2002 Feb 12; 41(6):1853-60. PubMed ID: 11827530
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  • 19. Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme.
    Fabiane SM, Sohi MK, Wan T, Payne DJ, Bateson JH, Mitchell T, Sutton BJ.
    Biochemistry; 1998 Sep 08; 37(36):12404-11. PubMed ID: 9730812
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  • 20. Substrate-activated zinc binding of metallo-beta -lactamases: physiological importance of mononuclear enzymes.
    Wommer S, Rival S, Heinz U, Galleni M, Frere JM, Franceschini N, Amicosante G, Rasmussen B, Bauer R, Adolph HW.
    J Biol Chem; 2002 Jul 05; 277(27):24142-7. PubMed ID: 11967267
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