| References: | 1. Fre`re, J. M. (1995) Beta-lactamases and bacterial resistance to
antibiotics, Mol. Microbiol. 16, 385-395.
2. Galleni, M., Lamotte-Brasseur, J., Rossolini, G. M., Spencer, J.,
Dideberg, O., and Fre`re, J. M. (2001) Standard numbering scheme
for class B â-lactamases, Antimicrob. Agents Chemother. 45, 660-
663.
3. Fabiane, S. M., Sohi, M. K., Wan, T., Payne, D. J., Bateson, J.
H., Mitchell, T., and Sutton, B. J. (1998) Crystal structure of the
zinc-dependent â-lactamase from Bacillus cereus at 1.9 Å
resolution: binuclear active site with features of a mononuclear
enzyme, Biochemistry 37, 12404-12411
4. Orellano, E. G., Girardini, J. E., Cricco, J. A., Ceccarelli, E. A.,
and Vila, A. J. (1998) Spectroscopic characterization of a binuclear
metal site in Bacillus cereus â-lactamase II, Biochemistry 37,
10173-10180.
5. Paul-Soto, R., Bauer, R., Fre`re, J. M., Galleni, M., Meyer-Klaucke,
W., Nolting, H., Rossolini, G. M., de Seny, D., Hernandez-
Valladares, M., Zeppezauer, M., and Adolph, H. W. (1999) Monoand
binuclear Zn2+-â-lactamase. Role of the conserved cysteine
in the catalytic mechanism, J. Biol. Chem. 274, 13242-13249.
6. Concha, N. O., Rasmussen, B. A., Bush, K., and Herzberg, O.
(1996) Crystal structure of the wide-spectrum binuclear zinc
â-lactamase from Bacteroides fragilis, Structure 4, 823-836.
7. Paul-Soto, R., Hernadez-Valladares, M., Galleni, M., Bauer, R.,
Zeppezauer, M., Fre`re, J. M., and Adolph, H. W. (1998) Monoand
binuclear Zn2+-â-lactamase from Bacteroides fragilis: catalytic
and structural roles of the zinc ions, FEBS Lett. 438, 137-
140.
8. Yang, Y., Keeney, D., Tang, X., Canfield, N., and Rasmussen, B.
A. (1999) Kinetic properties and metal content of the metallo-â
-lactamase CcrA harboring selective amino acid substitutions, J.
Biol. Chem. 274, 15706-15711.
9. Wang, Z., Fast, W., and Benkovic, S. J. (1999) On the mechanism
of the Bacteroides fragilis metallo-â-lactamase, Biochemistry 38,
10013-10023.
10. Laraki, N., Franceschini, N., Rossolini, G. M., Santucci, P.,
Meunier, C., de Pauw, E., Amicosante, G., Fre`re, J. M., and
Galleni, M. (1999) Biochemical characterisation of the Pseudomonas
aeruginosa 101/1477 metallo-â-lactamase IMP-1 produced
by Escherichia coli, Antimicrob. Agents Chemother. 43, 902-
906.
11. Haruta, S., Yamaguchi, H., Yamamoto, E. T., Eriguchi, Y.,
Nukaga, M., O’Hara, K., and Sawai, T. (2000) Functional analysis
of the active site of a metallo-â-lactamase proliferating in Japan,
Antimicrob. Agents Chemother. 44, 2304-2309.
12. Concha, N. O., Janson, C. A., Rowling, P., Pearson, S., Cheever,
C. A., Clarke, B. P., Lewis, C., Galleni, M., Fre`re, J. M., Payne,
D. J., Bateson, J. H., and Abdel-Meguid, S. S. (2000) Crystal
structure of the IMP-1 metallo â-lactamase from Pseudomonas
aeruginosa and its complex with a mercaptocarboxylate inhibitor:
binding determinants of a potent, broad-spectrum inhibitor,
Biochemistry 39, 4288-4298.
13. Garcia-Saez, I., Hopkins, J., Papamicael, C., Franceschini, N.,
Amicosante, G., Rossolini, G. M., Galleni, M., Fre`re, J. M., and
Dideberg, O. (2003) The 1.5-A Structure of Chryseobacterium
meningosepticum zinc â-Lactamase in complex with the inhibitor,
D-captopril, J. Biol. Chem. 278, 23868-23873.
14. Crowder, M. W., and Walsh, T. R. (1999) Structure and function
of metallo-â-lactamases, Recent Res. DeV. Antimicrob. Agents
Chemother. 3, 105-132.
15. Carfi, A., Duee, E., Galleni, M., Fre`re, J. M., and Dideberg, O.
(1998) 1.85 Å resolution structure of the zinc (II) â-lactamase
from Bacillus cereus, Acta Crystallogr., Sect. D 54, 313-323.
16. Carfi, A., Duee, E., Paul-Soto, R., Galleni, M., Fre`re, J. M., and
Dideberg, O. (1998) X-ray structure of the Zn(II) â-lactamase from
Bacteroides fragilis in an orthorhombic crystal form, Acta
Crystallogr., Sect. D 54, 45-57.
17. Concha, N. O., Rasmussen, B. A., Bush, K., and Herzberg, O.
(1997) Crystal structure of the cadmium- and mercury-substituted
metallo-â-lactamase from Bacteroides fragilis, Protein Sci. 6,
2671-2676.
18. Paul-Soto, R., Zeppezauer, M., Adolph, H. W., Galleni, M., Fre`re,
J. M., Carfi, A., Dideberg, O., Wouter, J., Hemmingsen, L., and
Bauer, R. (1999) Preference of Cd(II) and Zn(II) for the two metal
sites in Bacillus cereus â-lactamase II: a perturbed angular
correlation of ç-rays (PAC) spectroscopy study, Biochemistry 38,
16500-16506.
19. de Seny, D, Heinz, U., Wommer, S., Kiefer, M., Meyer-Klaucke,
W., Galleni, M., Fre`re, J. M., Bauer, R., and Adolph, H. W. (2001)
Metal ion binding and coordination geometry for wild type and
mutants of metallo-â-lactamase from Bacillus cereus 569/H/9
(BcII); a combined thermodynamic, kinetic and spectroscopic
approach, J. Biol. Chem. 276, 45065-45078.
20. Wommer, S., Rival, S., Heinz, U., Galleni, M., Fre`re, J. M.,
Franceschini, N., Amicosante, G., Rasmussen, B., Bauer, R., and
Adolph, H. W. (2002) Substrate activated zinc binding of metallo-
â-lactamases; physiological importance of the mononuclear
enzymes, J. Biol. Chem. 277, 24142-24147.
21. Crowder, M. W., Wang, Z., Franklin, S. L., Zovinka, E. P., and
Benkovic, S. J. (1996) Characterization of the metal-binding sites
of the â-lactamase from Bacteroides fragilis, Biochemistry 35,
12126-12132.
22. Fast, W., Wang, Z., and Benkovic, S. J. (2001) Familial mutations
and zinc stoichiometry determine the rate-limiting step of nitrocefin
hydrolysis by metallo-â-lactamase from Bacteroides fragilis,
Biochemistry 40, 1640-1650.
23. Mitic, N., Smith, S. J., Neves, A., Guddat, L. W., Gahan, L. R.,
and Schenk, G. (2006) The catalytic mechanisms of binuclear
metallohydrolases, Chem. ReV., in press. Weston, J. (2005) Mode
of action of bi- and trinuclear zinc hydrolases and their synthetic
analogues, Chem. ReV. 105, 2151-2174.
Enzyme Deactivation Due to Metal-Ion Dissociation Biochemistry, Vol. 45, No. 36, 2006 11019
24. Auld, D. S. (1995) Removal and replacement of metal ions in
metallopepatidases, Methods Enzymol. 248, 228-242. Maret, W.,
and Vallee, B. L. (1993) Cobalt as probe and label of proteins,
Methods Enzymol. 226, 52-71. Vila, A. J., and Fernandez, C. O.
(1997) Alkaline transition of Rhus Vernicifera stellacyanin, an
unusual blue copper protein, Biochemistry 36, 10566-10570. Guo,
J. Q., Wang, S. K., Dong, J., Qiu, H. W., Scott, R. A., and Giedroc,
D. P. (1995) X-ray and visible absorption spectroscopy of wildtype
and mutant T4 gene 32 proteins: His61, not His81 is the
nonthiolate zinc ligand, J. Am. Chem. Soc. 117, 9437-9440.
25. Bertini, I., Johnsson, B. H., Luchinat, C., Pierattelli, R., and Vila,
A. J. (1994) Strategies of signal assignments in paramagnetic
metalloproteins. An NMR investigation of the thiocyanate adduct
of the cobalt (II) substituted human carbonic anhydrase II, J.
Magn. Reson., Ser. B 104, 230-239. Oz, G., Pountney, D. L.,
and Armitage, I. M. (1998) NMR spectroscopic studies of I)1/2
metal ions in biological systems, Biochem. Cell Biol. 76, 223-
234. Bennet, B., and Holz, R. C. (1997) EPR studies on the monoand
dicobalt(II)-substituted forms of the aminopeptidase from
Aeromonas proteolytica. Insight into the catalytic mechanism of
dinuclear hydrolases, J. Am. Chem. Soc. 119, 1923-1933.
26. Bauer, R., Adolph, H. W., Andersson, I., Danielsen, E., Formicka,
G., and Zeppezauer, M. (1991) Coordination geometry for
cadmium in the catalytic zinc site of horse liver alcohol dehydrogenase:
studies by PAC spectroscopy, Eur. Biophys. J. 20,
215-221.
27. Bicknell, R., Knott-Hunziker, Y., and Waley, S. G. (1983) The
pH-dependence of class B and class C â-lactamases, Biochem. J.
213, 61-66.
28. Baldwin, G. S., Edwards, G. F. StL., Kiener, P. A., Tully, M. J.,
Waley, S. G., and Abraham, E. P. (1980) Production of a variant
of beta-lactamase II with selectively decreased cephalosporinase
activity by a mutant of Bacillus cereus 569/H/9, Biochem. J. 191,
111-116.
29. Hemmingsen, L., Damblon, C., Antony, J., Jensen, M., Adolph,
H. W., Wommer, S., Roberts, G. C. K., and Bauer, R. (2001)
Dynamics of mononuclear cadmium beta-lactamase revealed by
the combination of NMR and PAC spectroscopy, J. Am. Chem.
Soc. 123, 10329-10335.
30. Damblon, C., Jensen, M., Ababou, A., Barsukov, I., Papamicael,
C., Schofield, C. J., Olsen, L., Bauer, R., and Roberts, G. C. (2003)
The inhibitor thiomandelic acid binds to both metal ions in
metallo-beta-lactamase and induces positive cooperativity in metal
binding, J. Biol. Chem. 31, 29240-29251.
31. Wang, Z., and Benkovic, S. J. (1998) Purification, characterization,
and kinetic studies of a soluble Bacteroides fragilis metallo-â-
lactamase that provides multiple antibiotic resistance, J. Biol.
Chem. 273, 22402-22408.
32. Myers, J. L., and Shaw, R. W. (1989) Production, purification
and spectral properties of metal-dependent â-lactamase from
Bacillus cereus, Biochim. Biophys. Acta 995, 264-272.
33. Bicknell, R., and Waley, S. G. (1985) Cryoenzymology of Bacillus
cereus â-lactamase II, Biochemistry 24, 6876-6887.
34. Bicknell, R., Schaffer, A, Waley, S. G., and Auld, D. S. (1986)
Changes in the coordination geometry of the active-site metal
during catalysis of benzylpenicillin hydrolysis by Bacillus cereus
â-lactamase II, Biochemistry 25, 7208-7215.
35. Bounaga, S., Laws, A. P., Galleni, M., and Page, M. I. (1998)
The mechanism of catalysis and the inhibition of the Bacillus
cereus zinc-dependent â-lactamase, Biochem J. 331, 703-711.
36. Rasia, R. M., and Vila, A. J. (2004) Structural determinants of
substrate binding to Bacillus cereus metallo-â-lactamase, J. Biol.
Chem. 279, 26046-26051.
37. Schowen, K. B., and Schowen, R. L. (1982) Solvent isotope effects
on enzyme systems, Methods Enzymol. 87, 551-606.
38. Badarau, A. (2006) Reactivity and Inhibition of Metallo-â-
lactamases, Ph.D. Thesis, University of Huddersfield, Huddersfield,
U.K. |
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