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Volumn 107, Issue 6, 2014, Pages 1263-1272

X-ray absorption spectroscopy of dinuclear metallohydrolases

Author keywords

[No Author keywords available]

Indexed keywords

HYDROLASE; METAL;

EID: 84909619197     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2014.07.066     Document Type: Review
Times cited : (16)

References (104)
  • 1
    • 51149137229 scopus 로고
    • An X-ray absorption band
    • Bragg, W. H. 1914. An X-ray absorption band. Nature. 93:31-32.
    • (1914) Nature , vol.93 , pp. 31-32
    • Bragg, W.H.1
  • 2
    • 84909614781 scopus 로고
    • The fine structure of the discontinuities in X-ray absorption spectra
    • deBroglie, M., and A. Dauvillier. 1920. The fine structure of the discontinuities in X-ray absorption spectra. Compt. Rend. 171:626-627.
    • (1920) Compt. Rend. , vol.171 , pp. 626-627
    • DeBroglie, M.1    Dauvillier, A.2
  • 3
    • 0040202690 scopus 로고
    • The X-ray absorption spectra of chlorine
    • Lindh, A. E. 1921. The X-ray absorption spectra of chlorine. Compt. Rend. 172:1175-1176.
    • (1921) Compt. Rend. , vol.172 , pp. 1175-1176
    • Lindh, A.E.1
  • 4
    • 84909614780 scopus 로고
    • Mass-absorption coefficients as a function of wave length above and below the K X-ray limit of the absorber
    • Richtmyer, F. K. 1921. Mass-absorption coefficients as a function of wave length above and below the K X-ray limit of the absorber. Phys. Rev. 17:264-265.
    • (1921) Phys. Rev. , vol.17 , pp. 264-265
    • Richtmyer, F.K.1
  • 6
    • 0001617255 scopus 로고
    • Measurement of metal-ligand distances by EXAFS
    • Scott, R. A. 1985. Measurement of metal-ligand distances by EXAFS. Methods Enzymol. 117:414-459.
    • (1985) Methods Enzymol. , vol.117 , pp. 414-459
    • Scott, R.A.1
  • 7
    • 18544395945 scopus 로고
    • A new design for high flux grazing incidence monochromator for synchrotron radiation
    • Depautex, C., P. Thiry, ..., J. Flamand. 1978. A new design for high flux grazing incidence monochromator for synchrotron radiation. Nucl. Instrum. Methods. 152:101-102.
    • (1978) Nucl. Instrum. Methods , vol.152 , pp. 101-102
    • Depautex, C.1    Thiry, P.2    Flamand, J.3
  • 8
    • 0018469424 scopus 로고
    • X-ray monochromator development for synchrotron radiation facilities
    • Deslattes, R. D. 1980. X-ray monochromator development for synchrotron radiation facilities. Nucl. Instrum. Methods. 172:201-208.
    • (1980) Nucl. Instrum. Methods , vol.172 , pp. 201-208
    • Deslattes, R.D.1
  • 9
    • 0018470099 scopus 로고
    • X-ray monochromator geometry for focusing synchrotron radiation above 10 keV
    • Sparks, Jr., C. J., B. S. Borie, and J. B. Hastings. 1980. X-ray monochromator geometry for focusing synchrotron radiation above 10 keV. Nucl. Instrum. Methods. 172:237-242.
    • (1980) Nucl. Instrum. Methods , vol.172 , pp. 237-242
    • Sparks, C.J.1    Borie, B.S.2    Hastings, J.B.3
  • 10
    • 0019558240 scopus 로고
    • X-ray monochromator system for use with synchrotron radiation sources
    • Golovchenko, J. A., R. A. Levesque, and P. L. Cowan. 1981. X-ray monochromator system for use with synchrotron radiation sources. Rev. Sci. Instrum. 52:509-516.
    • (1981) Rev. Sci. Instrum. , vol.52 , pp. 509-516
    • Golovchenko, J.A.1    Levesque, R.A.2    Cowan, P.L.3
  • 11
    • 0021505766 scopus 로고
    • Measurement of soft x-ray absorption spectra with a fluorescent ion chamber detector
    • Lytle, F. W., R. B. Greegor, ..., F. E. Huggins. 1984. Measurement of soft x-ray absorption spectra with a fluorescent ion chamber detector. Nucl. Instrum. Methods Phys. Res. A. 226:542-548.
    • (1984) Nucl. Instrum. Methods Phys. Res. A , vol.226 , pp. 542-548
    • Lytle, F.W.1    Greegor, R.B.2    Huggins, F.E.3
  • 12
    • 0019539407 scopus 로고
    • New fluorescence detection system for x-ray absorption spectroscopy
    • Cramer, S. P., and R. A. Scott. 1981. New fluorescence detection system for x-ray absorption spectroscopy. Rev. Sci. Instrum. 52:395-399.
    • (1981) Rev. Sci. Instrum. , vol.52 , pp. 395-399
    • Cramer, S.P.1    Scott, R.A.2
  • 15
    • 0036521366 scopus 로고    scopus 로고
    • Fast multigrid fluorescent ion chamber with 0.1 ms time response
    • Suzuki, M., N. Kawamura, ..., T. Ishikawa. 2002. Fast multigrid fluorescent ion chamber with 0.1 ms time response. J. Synchrotron Radiat. 9:99-102.
    • (2002) J. Synchrotron Radiat. , vol.9 , pp. 99-102
    • Suzuki, M.1    Kawamura, N.2    Ishikawa, T.3
  • 16
    • 22244490160 scopus 로고
    • New technique for investigating noncrystalline structures: Fourier analysis of the extended x-ray-absorption fine structure
    • Sayers, D. E., E. A. Stern, and F. W. Lytle. 1971. New technique for investigating noncrystalline structures: Fourier analysis of the extended x-ray-absorption fine structure. Phys. Rev. Lett. 27:1204-1207.
    • (1971) Phys. Rev. Lett. , vol.27 , pp. 1204-1207
    • Sayers, D.E.1    Stern, E.A.2    Lytle, F.W.3
  • 17
    • 33751036780 scopus 로고
    • Extended x-ray-absorption fine-structure technique. III. Determination of physical parameters
    • Stern, E. A., D. E. Sayers, and F. W. Lytle. 1975. Extended x-ray-absorption fine-structure technique. III. Determination of physical parameters. Phys. Rev. B. 11:4836-4846.
    • (1975) Phys. Rev. B , vol.11 , pp. 4836-4846
    • Stern, E.A.1    Sayers, D.E.2    Lytle, F.W.3
  • 18
    • 0001965537 scopus 로고
    • X-ray absorption: Principles, applications, techniques of EXAFS, SEXAFS and XANES
    • D. C. Koningsberger, and R. Prins, editors. John Wiley & Sons, New York
    • Stern, E. A. 1988. X-ray absorption: principles, applications, techniques of EXAFS, SEXAFS and XANES. In Chemical Analysis, Vol. 92. D. C. Koningsberger, and R. Prins, editors. John Wiley & Sons, New York.
    • (1988) Chemical Analysis , vol.92
    • Stern, E.A.1
  • 19
    • 0001338205 scopus 로고
    • New high-energy approximation for x-ray-absorption near-edge structure
    • Rehr, J. J., R. C. Albers, ..., E. A. Stern. 1986. New high-energy approximation for x-ray-absorption near-edge structure. Phys. Rev. B Condens. Matter. 34:4350-4353.
    • (1986) Phys. Rev. B Condens. Matter. , vol.34 , pp. 4350-4353
    • Rehr, J.J.1    Albers, R.C.2    Stern, E.A.3
  • 20
    • 0024682639 scopus 로고
    • Spherical wave theories of EXAFS
    • Gurman, S. J. 1989. Spherical wave theories of EXAFS. Physica B. 158:359-361.
    • (1989) Physica B , vol.158 , pp. 359-361
    • Gurman, S.J.1
  • 21
    • 0000991396 scopus 로고
    • Comparison of theoretical methods for the calculation of extended x-ray-absorption fine structure
    • Vaarkamp, M., I. Dring, ..., D. C. Koningsberger. 1994. Comparison of theoretical methods for the calculation of extended x-ray-absorption fine structure. Phys. Rev. B Condens. Matter. 50:7872-7883.
    • (1994) Phys. Rev. B Condens. Matter. , vol.50 , pp. 7872-7883
    • Vaarkamp, M.1    Dring, I.2    Koningsberger, D.C.3
  • 22
    • 9644277158 scopus 로고    scopus 로고
    • State-of-the-art analysis of whole x-ray absorption spectra
    • Binsted, N., and S. S. Hasnain. 1996. State-of-the-art analysis of whole x-ray absorption spectra. J. Synchrotron Radiat. 3:185-196.
    • (1996) J. Synchrotron Radiat. , vol.3 , pp. 185-196
    • Binsted, N.1    Hasnain, S.S.2
  • 23
    • 77952922754 scopus 로고    scopus 로고
    • Parameter-free calculations of X-ray spectra with FEFF9
    • Rehr, J. J., J. J. Kas, ..., K. Jorissen. 2010. Parameter-free calculations of X-ray spectra with FEFF9. Phys. Chem. Chem. Phys. 12:5503-5513.
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 5503-5513
    • Rehr, J.J.1    Kas, J.J.2    Jorissen, K.3
  • 25
    • 0033303217 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy in coordination chemistry
    • Penner-Hahn, J. E. 1999. X-ray absorption spectroscopy in coordination chemistry. Coord. Chem. Rev. 190-192:1101-1123.
    • (1999) Coord. Chem. Rev. , vol.190-192 , pp. 1101-1123
    • Penner-Hahn, J.E.1
  • 26
    • 11144335218 scopus 로고    scopus 로고
    • Characterization of "spectroscopically quiet" metals in biology
    • Penner-Hahn, J. E. 2005. Characterization of "spectroscopically quiet" metals in biology. Coord. Chem. Rev. 249:161-177.
    • (2005) Coord. Chem. Rev. , vol.249 , pp. 161-177
    • Penner-Hahn, J.E.1
  • 27
    • 0037208355 scopus 로고    scopus 로고
    • Experimental aspects of biological X-ray absorption spectroscopy
    • Ascone, I., W. Meyer-Klaucke, and L. Murphy. 2003. Experimental aspects of biological X-ray absorption spectroscopy. J. Synchrotron Radiat. 10:16-22.
    • (2003) J. Synchrotron Radiat. , vol.10 , pp. 16-22
    • Ascone, I.1    Meyer-Klaucke, W.2    Murphy, L.3
  • 28
    • 11144309505 scopus 로고    scopus 로고
    • Progress in the theory and interpretation of XANES
    • Rehr, J. J., and A. L. Ankudinov. 2005. Progress in the theory and interpretation of XANES. Coord. Chem. Rev. 249:131-140.
    • (2005) Coord. Chem. Rev. , vol.249 , pp. 131-140
    • Rehr, J.J.1    Ankudinov, A.L.2
  • 29
    • 0001596121 scopus 로고    scopus 로고
    • Theoretical analysis of x-ray absorption near-edge structure of transition-metal aqueous complexes in solution at the metal K edge
    • Benfatto, M., J. A. Solera, ..., J. Garcia. 1997. Theoretical analysis of x-ray absorption near-edge structure of transition-metal aqueous complexes in solution at the metal K edge. Phys. Rev. B. 56:2447-2452.
    • (1997) Phys. Rev. B , vol.56 , pp. 2447-2452
    • Benfatto, M.1    Solera, J.A.2    Garcia, J.3
  • 30
    • 4243708060 scopus 로고    scopus 로고
    • Calculation and interpretation of K-shell X-ray absorption near-edge structure of transition metal oxides
    • Modrow, H., S. Bucher, J. J. Rehr, and A. L. Ankudinov. 2003. Calculation and interpretation of K-shell X-ray absorption near-edge structure of transition metal oxides. Phys. Rev. B. 67:035123.
    • (2003) Phys. Rev. B , vol.67 , pp. 035123
    • Modrow, H.1    Bucher, S.2    Rehr, J.J.3    Ankudinov, A.L.4
  • 31
    • 56649100528 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy of hemes and hemeproteins in solution: Multiple scattering analysis
    • D'Angelo, P., A. Lapi, ..., S. Della-Longa. 2008. X-ray absorption spectroscopy of hemes and hemeproteins in solution: multiple scattering analysis. Inorg. Chem. 47:9905-9918.
    • (2008) Inorg. Chem. , vol.47 , pp. 9905-9918
    • D'Angelo, P.1    Lapi, A.2    Della-Longa, S.3
  • 32
    • 0001352661 scopus 로고
    • X-ray absorption studies of high-spin iron(II) complexes
    • Randall, C. R., L. Shu, ..., L. Que, Jr. 1995. X-ray absorption studies of high-spin iron(II) complexes. Inorg. Chem. 34:1036-1039.
    • (1995) Inorg. Chem. , vol.34 , pp. 1036-1039
    • Randall, C.R.1    Shu, L.2    Que, L.3
  • 33
    • 0000788131 scopus 로고
    • X-ray absorption spectroscopy of iron-tyrosinate proteins
    • Roe, A. L., D. J. Schneider, ..., L. Que, Jr. 1984. X-ray absorption spectroscopy of iron-tyrosinate proteins. J. Am. Chem. Soc. 106:1676-1681.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 1676-1681
    • Roe, A.L.1    Schneider, D.J.2    Que, L.3
  • 34
    • 0001727482 scopus 로고
    • X-ray absorption edge spectrometry as applied to coordination chemistry
    • Srivastava, U. C., and H. L. Nigam. 1972. X-ray absorption edge spectrometry as applied to coordination chemistry. Coord. Chem. Rev. 9:275-310.
    • (1972) Coord. Chem. Rev. , vol.9 , pp. 275-310
    • Srivastava, U.C.1    Nigam, H.L.2
  • 35
    • 0028938504 scopus 로고
    • X-ray absorption spectroscopy of the iron site in Escherichia coli Fe(III) superoxide dismutase
    • Tierney, D. L., J. A. Fee, ..., J. E. Penner-Hahn. 1995. X-ray absorption spectroscopy of the iron site in Escherichia coli Fe(III) superoxide dismutase. Biochemistry. 34:1661-1668.
    • (1995) Biochemistry , vol.34 , pp. 1661-1668
    • Tierney, D.L.1    Fee, J.A.2    Penner-Hahn, J.E.3
  • 36
    • 0026320120 scopus 로고
    • Inactivation and reactivation of manganese catalase: Oxidation-state assignments using X-ray absorption spectroscopy
    • Waldo, G. S., R. M. Fronko, and J. E. Penner-Hahn. 1991. Inactivation and reactivation of manganese catalase: oxidation-state assignments using X-ray absorption spectroscopy. Biochemistry. 30:10486-10490.
    • (1991) Biochemistry , vol.30 , pp. 10486-10490
    • Waldo, G.S.1    Fronko, R.M.2    Penner-Hahn, J.E.3
  • 38
    • 0030857696 scopus 로고    scopus 로고
    • EXAFS comparison of the dimanganese core structures of manganese catalase, arginase, and manganese-substituted ribonucleotide reductase and hemerythrin
    • Stemmler, T. L., T. M. Sossong, Jr., ..., J. E. Penner-Hahn. 1997. EXAFS comparison of the dimanganese core structures of manganese catalase, arginase, and manganese-substituted ribonucleotide reductase and hemerythrin. Biochemistry. 36:9847-9858.
    • (1997) Biochemistry , vol.36 , pp. 9847-9858
    • Stemmler, T.L.1    Sossong, T.M.2    Penner-Hahn, J.E.3
  • 39
    • 0005138378 scopus 로고
    • Structure diversity of F430 from Methanobacterium thermoautotrophicum. A nickel x-ray absorption spectroscopic study
    • Eidsness, M. K., R. J. Sullivan, ..., R. A. Scott. 1986. Structure diversity of F430 from Methanobacterium thermoautotrophicum. A nickel x-ray absorption spectroscopic study. J. Am. Chem. Soc. 108:3120-3121.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 3120-3121
    • Eidsness, M.K.1    Sullivan, R.J.2    Scott, R.A.3
  • 40
    • 0000111635 scopus 로고
    • 2 chromophores and spectroscopic studies on hydride and carbon monoxide binding at these nickel centers: Relevance to the reactivity of the nickel site(s) in [FeNi] hydrogenases
    • 2 chromophores and spectroscopic studies on hydride and carbon monoxide binding at these nickel centers: relevance to the reactivity of the nickel site(s) in [FeNi] hydrogenases. Inorg. Chem. 31:3612-3619.
    • (1992) Inorg. Chem. , vol.31 , pp. 3612-3619
    • Baidya, N.1    Olmstead, M.M.2    Mascharak, P.K.3
  • 41
    • 42549166211 scopus 로고    scopus 로고
    • 2 complexes using sulfur K-edge and nickel L-edge X-ray absorption spectroscopies: Implications for the active site of nickel superoxide dismutase
    • 2 complexes using sulfur K-edge and nickel L-edge X-ray absorption spectroscopies: implications for the active site of nickel superoxide dismutase. Inorg. Chem. 47:2649-2660.
    • (2008) Inorg. Chem. , vol.47 , pp. 2649-2660
    • Shearer, J.1    Dehestani, A.2    Abanda, F.3
  • 42
    • 0000774586 scopus 로고
    • Bond valence sum analysis of metal-ligand bond lengths in metalloenzymes and model complexes
    • Thorp, H. H. 1992. Bond valence sum analysis of metal-ligand bond lengths in metalloenzymes and model complexes. Inorg. Chem. 31:1585-1588.
    • (1992) Inorg. Chem. , vol.31 , pp. 1585-1588
    • Thorp, H.H.1
  • 43
    • 13144307055 scopus 로고    scopus 로고
    • Spectroscopic identification of a dinuclear metal centre in manganese(II)-activated aminopeptidase P from Escherichia coli: Implications for human prolidase
    • Zhang, L., M. J. Crossley, ..., H. C. Freeman. 1998. Spectroscopic identification of a dinuclear metal centre in manganese(II)-activated aminopeptidase P from Escherichia coli: implications for human prolidase. J. Biol. Inorg. Chem. 3:470-483.
    • (1998) J. Biol. Inorg. Chem. , vol.3 , pp. 470-483
    • Zhang, L.1    Crossley, M.J.2    Freeman, H.C.3
  • 44
    • 0035818432 scopus 로고    scopus 로고
    • Structural evidence that the methionyl aminopeptidase from Escherichia coli is a mononuclear metalloprotease
    • Cosper, N. J., V. M. D'souza, ..., R. C. Holz. 2001. Structural evidence that the methionyl aminopeptidase from Escherichia coli is a mononuclear metalloprotease. Biochemistry. 40:13302-13309.
    • (2001) Biochemistry , Issue.40 , pp. 13302-13309
    • Cosper, N.J.1    D'souza, V.M.2    Holz, R.C.3
  • 45
    • 0037474241 scopus 로고    scopus 로고
    • Characterization of the zinc-binding site of the histidine-proline-rich glycoprotein associated with rabbit skeletal muscle AMP deaminase
    • Mangani, S., W. Meyer-Klaucke, ..., A. Raggi. 2003. Characterization of the zinc-binding site of the histidine-proline-rich glycoprotein associated with rabbit skeletal muscle AMP deaminase. J. Biol. Chem. 278:3176-3184.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3176-3184
    • Mangani, S.1    Meyer-Klaucke, W.2    Raggi, A.3
  • 46
    • 33846781046 scopus 로고    scopus 로고
    • Characterization of the metallocenter of rabbit skeletal muscle AMP deaminase. Evidence for a dinuclear zinc site
    • Mangani, S., M. Benvenuti, ..., A. Raggi. 2007. Characterization of the metallocenter of rabbit skeletal muscle AMP deaminase. Evidence for a dinuclear zinc site. Biochim. Biophys. Acta. 1774:312-322.
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 312-322
    • Mangani, S.1    Benvenuti, M.2    Raggi, A.3
  • 47
    • 36849045183 scopus 로고    scopus 로고
    • Characterization of the metallocenter of rabbit skeletal muscle AMP deaminase. A new model for substrate interactions at a dinuclear cocatalytic Zn site
    • Martini, D., M. Ranieri-Raggi, ..., A. Raggi. 2007. Characterization of the metallocenter of rabbit skeletal muscle AMP deaminase. A new model for substrate interactions at a dinuclear cocatalytic Zn site. Biochim. Biophys. Acta. 1774:1508-1518.
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 1508-1518
    • Martini, D.1    Ranieri-Raggi, M.2    Raggi, A.3
  • 48
    • 77952092254 scopus 로고    scopus 로고
    • Identifying the structure of the active sites of human recombinant prolidase
    • Besio, R., S. Alleva, ..., S. Morante. 2010. Identifying the structure of the active sites of human recombinant prolidase. Eur. Biophys. J. 39:935-945.
    • (2010) Eur. Biophys. J. , vol.39 , pp. 935-945
    • Besio, R.1    Alleva, S.2    Morante, S.3
  • 49
    • 0345293205 scopus 로고    scopus 로고
    • The dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase from Haemophilus influenzae is a dinuclear metallohydrolase
    • Cosper, N. J., D. L. Bienvenue, ..., R. C. Holz. 2003. The dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase from Haemophilus influenzae is a dinuclear metallohydrolase. J. Am. Chem. Soc. 125:14654-14655.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14654-14655
    • Cosper, N.J.1    Bienvenue, D.L.2    Holz, R.C.3
  • 50
    • 77950003784 scopus 로고    scopus 로고
    • Replacing Mn(2+) with Co(2+) in human arginase I enhances cytotoxicity toward l-arginine auxotrophic cancer cell lines
    • Stone, E. M., E. S. Glazer, ..., G. Georgiou. 2010. Replacing Mn(2+) with Co(2+) in human arginase I enhances cytotoxicity toward l-arginine auxotrophic cancer cell lines. ACS Chem. Biol. 5:333-342.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 333-342
    • Stone, E.M.1    Glazer, E.S.2    Georgiou, G.3
  • 51
    • 33750695657 scopus 로고    scopus 로고
    • The quorum-quenching metallo-γ-lactonase from Bacillus thuringiensis exhibits a leaving group thio effect
    • Momb, J., P. W. Thomas, ..., W. Fast. 2006. The quorum-quenching metallo-γ-lactonase from Bacillus thuringiensis exhibits a leaving group thio effect. Biochemistry. 45:13385-13393.
    • (2006) Biochemistry , vol.45 , pp. 13385-13393
    • Momb, J.1    Thomas, P.W.2    Fast, W.3
  • 52
    • 18844433603 scopus 로고    scopus 로고
    • The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein
    • Thomas, P. W., E. M. Stone, ..., W. Fast. 2005. The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein. Biochemistry. 44:7559-7569.
    • (2005) Biochemistry , vol.44 , pp. 7559-7569
    • Thomas, P.W.1    Stone, E.M.2    Fast, W.3
  • 53
    • 0037047388 scopus 로고    scopus 로고
    • ElaC encodes a novel binuclear zinc phosphodiesterase
    • Vogel, A., O. Schilling, ..., W. Meyer-Klaucke. 2002. ElaC encodes a novel binuclear zinc phosphodiesterase. J. Biol. Chem. 277:29078-29085.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29078-29085
    • Vogel, A.1    Schilling, O.2    Meyer-Klaucke, W.3
  • 54
    • 3142738641 scopus 로고    scopus 로고
    • Identification of metal binding residues for the binuclear zinc phosphodiesterase reveals identical coordination as glyoxalase II
    • Vogel, A., O. Schilling, and W. Meyer-Klaucke. 2004. Identification of metal binding residues for the binuclear zinc phosphodiesterase reveals identical coordination as glyoxalase II. Biochemistry. 43:10379-10386.
    • (2004) Biochemistry , vol.43 , pp. 10379-10386
    • Vogel, A.1    Schilling, O.2    Meyer-Klaucke, W.3
  • 55
    • 12844249496 scopus 로고    scopus 로고
    • Zinc- and iron-dependent cytosolic metallo-β-lactamase domain proteins exhibit similar zinc-binding affinities, independent of an atypical glutamate at the metal-binding site
    • Schilling, O., A. Vogel, ..., W. Meyer-Klaucke. 2005. Zinc- and iron-dependent cytosolic metallo-β-lactamase domain proteins exhibit similar zinc-binding affinities, independent of an atypical glutamate at the metal-binding site. Biochem. J. 385:145-153.
    • (2005) Biochem. J. , vol.385 , pp. 145-153
    • Schilling, O.1    Vogel, A.2    Meyer-Klaucke, W.3
  • 56
    • 37349084962 scopus 로고    scopus 로고
    • Metal requirements and phosphodiesterase activity of tRNase Z enzymes
    • Späth, B., F. Settele, ..., A. Marchfelder. 2007. Metal requirements and phosphodiesterase activity of tRNase Z enzymes. Biochemistry. 46:14742-14750.
    • (2007) Biochemistry , vol.46 , pp. 14742-14750
    • Späth, B.1    Settele, F.2    Marchfelder, A.3
  • 57
    • 0141928715 scopus 로고    scopus 로고
    • Flexible metal binding of the metallo-β-lactamase domain: Glyoxalase II incorporates iron, manganese, and zinc in vivo
    • Schilling, O., N. Wenzel, ..., W. Meyer-Klaucke. 2003. Flexible metal binding of the metallo-β-lactamase domain: glyoxalase II incorporates iron, manganese, and zinc in vivo. Biochemistry. 42:11777-11786.
    • (2003) Biochemistry , vol.42 , pp. 11777-11786
    • Schilling, O.1    Wenzel, N.2    Meyer-Klaucke, W.3
  • 58
    • 3042753332 scopus 로고    scopus 로고
    • The binding of iron and zinc to glyoxalase II occurs exclusively as di-metal centers and is unique within the metallo-β-lactamase family
    • Wenzel, N. F., A. L. Carenbauer, ..., M. W. Crowder. 2004. The binding of iron and zinc to glyoxalase II occurs exclusively as di-metal centers and is unique within the metallo-β-lactamase family. J. Biol. Inorg. Chem. 9:429-438.
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 429-438
    • Wenzel, N.F.1    Carenbauer, A.L.2    Crowder, M.W.3
  • 59
    • 44049116699 scopus 로고
    • EXAFS study of the active site of alkaline phosphatase from E. coli
    • Mangani, S., P. Carloni, ..., J. E. Coleman. 1992. EXAFS study of the active site of alkaline phosphatase from E. coli. Inorg. Chim. Acta. 191:161-165.
    • (1992) Inorg. Chim. Acta , vol.191 , pp. 161-165
    • Mangani, S.1    Carloni, P.2    Coleman, J.E.3
  • 60
    • 33748502826 scopus 로고    scopus 로고
    • The catalytic mechanisms of binuclear metallohydrolases
    • Mitić, N., S. J. Smith, ..., G. Schenk. 2006. The catalytic mechanisms of binuclear metallohydrolases. Chem. Rev. 106:3338-3363.
    • (2006) Chem. Rev. , vol.106 , pp. 3338-3363
    • Mitić, N.1    Smith, S.J.2    Schenk, G.3
  • 61
    • 77954290084 scopus 로고    scopus 로고
    • Feeding hungry plants: The role of purple acid phosphatases in phosphate nutrition
    • Tran, H. T., B. A. Hurley, and W. C. Plaxtona. 2010. Feeding hungry plants: the role of purple acid phosphatases in phosphate nutrition. Plant Sci. 179:14-27.
    • (2010) Plant Sci. , vol.179 , pp. 14-27
    • Tran, H.T.1    Hurley, B.A.2    Plaxtona, W.C.3
  • 62
    • 0001417650 scopus 로고
    • X-ray absorption studies on the purple acid phosphatase from beef spleen
    • Kauzlarich, S. M., B. K. Teo, ..., B. A. Averill. 1986. X-ray absorption studies on the purple acid phosphatase from beef spleen. Inorg. Chem. 25:2781-2785.
    • (1986) Inorg. Chem. , vol.25 , pp. 2781-2785
    • Kauzlarich, S.M.1    Teo, B.K.2    Averill, B.A.3
  • 63
    • 0030596529 scopus 로고    scopus 로고
    • Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures
    • Klabunde, T., N. Sträter, ..., B. Krebs. 1996. Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures. J. Mol. Biol. 259:737-748.
    • (1996) J. Mol. Biol. , vol.259 , pp. 737-748
    • Klabunde, T.1    Sträter, N.2    Krebs, B.3
  • 64
    • 0033565606 scopus 로고    scopus 로고
    • Crystal structure of mammalian purple acid phosphatase
    • Guddat, L. W., A. S. McAlpine, ..., J. L. Martin. 1999. Crystal structure of mammalian purple acid phosphatase. Structure. 7:757-767.
    • (1999) Structure , vol.7 , pp. 757-767
    • Guddat, L.W.1    McAlpine, A.S.2    Martin, J.L.3
  • 65
    • 0000345359 scopus 로고
    • EXAFS studies of uteroferrin and its anion complexes
    • True, A. E., R. C. Scarrow, ..., L. Que, Jr. 1993. EXAFS studies of uteroferrin and its anion complexes. J. Am. Chem. Soc. 115:4246-4255.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 4246-4255
    • True, A.E.1    Scarrow, R.C.2    Que, L.3
  • 66
    • 0029989358 scopus 로고    scopus 로고
    • X-ray absorption spectroscopic studies of the FeZn derivative of uteroferrin
    • Wang, X., C. R. Randall, ..., L. Que, Jr. 1996. X-ray absorption spectroscopic studies of the FeZn derivative of uteroferrin. Biochemistry. 35:13946-13954.
    • (1996) Biochemistry , vol.35 , pp. 13946-13954
    • Wang, X.1    Randall, C.R.2    Que, L.3
  • 67
    • 0032568594 scopus 로고    scopus 로고
    • Extended X-ray absorption fine structure studies of the anion complexes of FeZn uteroferrin
    • Wang, X., and L. Que, Jr. 1998. Extended X-ray absorption fine structure studies of the anion complexes of FeZn uteroferrin. Biochemistry. 37:7813-7821.
    • (1998) Biochemistry , vol.37 , pp. 7813-7821
    • Wang, X.1    Que, L.2
  • 68
    • 0032829740 scopus 로고    scopus 로고
    • Spectroscopic characterization of a ternary phosphatase-substrate-fluoride complex. Mechanistic implications for dinuclear hydrolases
    • Wang, X., R. Y. N. Ho, ..., L. Que, Jr. 1999. Spectroscopic characterization of a ternary phosphatase-substrate-fluoride complex. Mechanistic implications for dinuclear hydrolases. J. Am. Chem. Soc. 121:9235-9236.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9235-9236
    • Wang, X.1    Ho, R.Y.N.2    Que, L.3
  • 69
    • 36649018684 scopus 로고    scopus 로고
    • Probing the role of the divalent metal ion in uteroferrin using metal ion replacement and a comparison to isostructural biomimetics
    • Schenk, G., R. A. Peralta, ..., A. Neves. 2008. Probing the role of the divalent metal ion in uteroferrin using metal ion replacement and a comparison to isostructural biomimetics. J. Biol. Inorg. Chem. 13:139-155.
    • (2008) J. Biol. Inorg. Chem. , vol.13 , pp. 139-155
    • Schenk, G.1    Peralta, R.A.2    Neves, A.3
  • 70
    • 14844366787 scopus 로고    scopus 로고
    • Introduction: Antibiotic resistance
    • Walsh, C., and G. Wright. 2005. Introduction: antibiotic resistance. Chem. Rev. 105:391-394.
    • (2005) Chem. Rev. , vol.105 , pp. 391-394
    • Walsh, C.1    Wright, G.2
  • 71
    • 33750624074 scopus 로고    scopus 로고
    • Metallo-β-lactamases: Novel weaponry for antibiotic resistance in bacteria
    • Crowder, M. W., J. Spencer, and A. J. Vila. 2006. Metallo-β-lactamases: novel weaponry for antibiotic resistance in bacteria. Acc. Chem. Res. 39:721-728.
    • (2006) Acc. Chem. Res. , vol.39 , pp. 721-728
    • Crowder, M.W.1    Spencer, J.2    Vila, A.J.3
  • 72
    • 11244317355 scopus 로고    scopus 로고
    • Metallo-β-lactamases: Two binding sites for one catalytic metal ion?
    • Heinz, U., and H. W. Adolph. 2004. Metallo-β-lactamases: two binding sites for one catalytic metal ion? Cell. Mol. Life Sci. 61:2827-2839.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 2827-2839
    • Heinz, U.1    Adolph, H.W.2
  • 73
    • 34948859355 scopus 로고    scopus 로고
    • Metallo-β-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily
    • Bebrone, C. 2007. Metallo-β-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily. Biochem. Pharmacol. 74:1686-1701.
    • (2007) Biochem. Pharmacol. , vol.74 , pp. 1686-1701
    • Bebrone, C.1
  • 75
    • 0033531792 scopus 로고    scopus 로고
    • 2+-β-lactamase. Role of the conserved cysteine in the catalytic mechanism
    • 2+-β-lactamase. Role of the conserved cysteine in the catalytic mechanism. J. Biol. Chem. 274:13242-13249.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13242-13249
    • Paul-Soto, R.1    Bauer, R.2    Adolph, H.W.3
  • 76
    • 0035976958 scopus 로고    scopus 로고
    • Metal ion binding and coordination geometry for wild type and mutants of metallo-β-lactamase from Bacillus cereus 569/H/9 (BcII): A combined thermodynamic, kinetic, and spectroscopic approach
    • de Seny, D., U. Heinz, ..., H. W. Adolph. 2001. Metal ion binding and coordination geometry for wild type and mutants of metallo-β-lactamase from Bacillus cereus 569/H/9 (BcII): a combined thermodynamic, kinetic, and spectroscopic approach. J. Biol. Chem. 276:45065-45078.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45065-45078
    • De Seny, D.1    Heinz, U.2    Adolph, H.W.3
  • 77
    • 35148836146 scopus 로고    scopus 로고
    • The Zn2 position in metallo-β-lactamases is critical for activity: A study on chimeric metal sites on a conserved protein scaffold
    • González, J. M., F. J. Medrano Martín, ..., A. J. Vila. 2007. The Zn2 position in metallo-β-lactamases is critical for activity: a study on chimeric metal sites on a conserved protein scaffold. J. Mol. Biol. 373:1141-1156.
    • (2007) J. Mol. Biol. , vol.373 , pp. 1141-1156
    • González, J.M.1    Medrano Martín, F.J.2    Vila, A.J.3
  • 78
    • 49749094732 scopus 로고    scopus 로고
    • Engineered mononuclear variants in Bacillus cereus metallo-β-lactamase BcII are inactive
    • Abriata, L. A., L. J. González, ..., A. J. Vila. 2008. Engineered mononuclear variants in Bacillus cereus metallo-β-lactamase BcII are inactive. Biochemistry. 47:8590-8599.
    • (2008) Biochemistry , vol.47 , pp. 8590-8599
    • Abriata, L.A.1    González, L.J.2    Vila, A.J.3
  • 79
    • 78649942815 scopus 로고    scopus 로고
    • Spectroscopic signature of a ubiquitous metal binding site in the metallo-β-lactamase superfamily
    • Campos-Bermudez, V. A., J. M. González, ..., A. J. Vila. 2010. Spectroscopic signature of a ubiquitous metal binding site in the metallo-β-lactamase superfamily. J. Biol. Inorg. Chem. 15:1209-1218.
    • (2010) J. Biol. Inorg. Chem. , vol.15 , pp. 1209-1218
    • Campos-Bermudez, V.A.1    González, J.M.2    Vila, A.J.3
  • 80
    • 56749107392 scopus 로고    scopus 로고
    • Metal content and localization during turnover in B. cereus metallo-β-lactamase
    • Llarrull, L. I., M. F. Tioni, and A. J. Vila. 2008. Metal content and localization during turnover in B. cereus metallo-β-lactamase. J. Am. Chem. Soc. 130:15842-15851.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 15842-15851
    • Llarrull, L.I.1    Tioni, M.F.2    Vila, A.J.3
  • 81
    • 35648968634 scopus 로고    scopus 로고
    • Evidence for a dinuclear active site in the metallo-β-lactamase BcII with substoichiometric Co(II). A new model for metal uptake
    • Llarrull, L. I., M. F. Tioni, ..., A. J. Vila. 2007. Evidence for a dinuclear active site in the metallo-β-lactamase BcII with substoichiometric Co(II). A new model for metal uptake. J. Biol. Chem. 282:30586-30595.
    • (2007) J. Biol. Chem. , vol.282 , pp. 30586-30595
    • Llarrull, L.I.1    Tioni, M.F.2    Vila, A.J.3
  • 82
    • 84861990698 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus
    • Breece, R. M., L. I. Llarrull, ..., D. L. Tierney. 2012. X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus. J. Inorg. Biochem. 111:182-186.
    • (2012) J. Inorg. Biochem. , vol.111 , pp. 182-186
    • Breece, R.M.1    Llarrull, L.I.2    Tierney, D.L.3
  • 83
    • 80054999128 scopus 로고    scopus 로고
    • Structural and kinetic studies on metallo-β-lactamase IMP-1
    • Griffin, D. H., T. K. Richmond, ..., M. W. Crowder. 2011. Structural and kinetic studies on metallo-β-lactamase IMP-1. Biochemistry. 50:9125-9134.
    • (2011) Biochemistry , vol.50 , pp. 9125-9134
    • Griffin, D.H.1    Richmond, T.K.2    Crowder, M.W.3
  • 84
    • 84901049657 scopus 로고    scopus 로고
    • Spectroscopic and mechanistic studies of heterodimetallic forms of metallo-β-lactamase NDM-1
    • Yang, H., M. Aitha, ..., D. L. Tierney. 2014. Spectroscopic and mechanistic studies of heterodimetallic forms of metallo-β-lactamase NDM-1. J. Am. Chem. Soc. 136:7273-7285.
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 7273-7285
    • Yang, H.1    Aitha, M.2    Tierney, D.L.3
  • 85
    • 31644444386 scopus 로고    scopus 로고
    • Sequential binding of cobalt(II) to metallo-β-lactamase CcrA
    • Periyannan, G. R., A. L. Costello, ..., M. W. Crowder. 2006. Sequential binding of cobalt(II) to metallo-β-lactamase CcrA. Biochemistry. 45:1313-1320.
    • (2006) Biochemistry , vol.45 , pp. 1313-1320
    • Periyannan, G.R.1    Costello, A.L.2    Crowder, M.W.3
  • 86
    • 68049106377 scopus 로고    scopus 로고
    • Differential binding of Co(II) and Zn(II) to metallo-β-lactamase Bla2 from Bacillus anthracis
    • Hawk, M. J., R. M. Breece, ..., M. W. Crowder. 2009. Differential binding of Co(II) and Zn(II) to metallo-β-lactamase Bla2 from Bacillus anthracis. J. Am. Chem. Soc. 131:10753-10762.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 10753-10762
    • Hawk, M.J.1    Breece, R.M.2    Crowder, M.W.3
  • 87
    • 33645551841 scopus 로고    scopus 로고
    • Site-selective binding of Zn(II) to metallo-β-lactamase L1 from Stenotrophomonas maltophilia
    • Costello, A., G. Periyannan, ..., D. L. Tierney. 2006. Site-selective binding of Zn(II) to metallo-β-lactamase L1 from Stenotrophomonas maltophilia. J. Biol. Inorg. Chem. 11:351-358.
    • (2006) J. Biol. Inorg. Chem. , vol.11 , pp. 351-358
    • Costello, A.1    Periyannan, G.2    Tierney, D.L.3
  • 88
    • 33750970568 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy of the zinc-binding sites in the class B2 metallo-β-lactamase ImiS from Aeromonas veronii bv. sobria
    • Costello, A. L., N. P. Sharma, ..., D. L. Tierney. 2006. X-ray absorption spectroscopy of the zinc-binding sites in the class B2 metallo-β-lactamase ImiS from Aeromonas veronii bv. sobria. Biochemistry. 45:13650-13658.
    • (2006) Biochemistry , vol.45 , pp. 13650-13658
    • Costello, A.L.1    Sharma, N.P.2    Tierney, D.L.3
  • 89
    • 46049100791 scopus 로고    scopus 로고
    • Conformational changes in the metallo-β-lactamase ImiS during the catalytic reaction: An EPR spectrokinetic study of Co(II)-spin label interactions
    • Sharma, N., Z. Hu, ..., B. Bennett. 2008. Conformational changes in the metallo-β-lactamase ImiS during the catalytic reaction: an EPR spectrokinetic study of Co(II)-spin label interactions. J. Am. Chem. Soc. 130:8215-8222.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 8215-8222
    • Sharma, N.1    Hu, Z.2    Bennett, B.3
  • 90
    • 69049101137 scopus 로고    scopus 로고
    • Motion of the zinc ions in catalysis by a dizinc metallo-β-lactamase
    • Breece, R. M., Z. Hu, ..., D. L. Tierney. 2009. Motion of the zinc ions in catalysis by a dizinc metallo-β-lactamase. J. Am. Chem. Soc. 131:11642-11643.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 11642-11643
    • Breece, R.M.1    Hu, Z.2    Tierney, D.L.3
  • 91
    • 84860753549 scopus 로고    scopus 로고
    • Mechanistic and spectroscopic studies of metallo-β-lactamase NDM-1
    • Yang, H., M. Aitha, ..., M. W. Crowder. 2012. Mechanistic and spectroscopic studies of metallo-β-lactamase NDM-1. Biochemistry. 51:3839-3847.
    • (2012) Biochemistry , vol.51 , pp. 3839-3847
    • Yang, H.1    Aitha, M.2    Crowder, M.W.3
  • 93
    • 0000059498 scopus 로고
    • Theory of extended x-ray absorption edge fine structure (EXAFS) in crystalline solids
    • Ashley, C. A., and S. Doniach. 1975. Theory of extended x-ray absorption edge fine structure (EXAFS) in crystalline solids. Phys. Rev. B. 11:1279-1288.
    • (1975) Phys. Rev. B , vol.11 , pp. 1279-1288
    • Ashley, C.A.1    Doniach, S.2
  • 94
    • 84909614779 scopus 로고    scopus 로고
    • note
    • Reference deleted in proof.
  • 95
    • 0028766307 scopus 로고
    • Extended x-ray absorption fine structure (EXAFS) analysis of disorder and multiple-scattering in complex crystalline solids
    • O'Day, P. A., J. J. Rehr, ..., G. E. Brown, Jr. 1994. Extended x-ray absorption fine structure (EXAFS) analysis of disorder and multiple-scattering in complex crystalline solids. J. Am. Chem. Soc. 116:2938-2949.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 2938-2949
    • O'Day, P.A.1    Rehr, J.J.2    Brown, G.E.3
  • 96
    • 0542395209 scopus 로고    scopus 로고
    • Real space multiple scattering calculation and interpretation of XANES
    • Ankudinov, A. L., B. Ravel, ..., S. D. Conradson. 1998. Real space multiple scattering calculation and interpretation of XANES. Phys. Rev. B. 58:7565-7576.
    • (1998) Phys. Rev. B , vol.58 , pp. 7565-7576
    • Ankudinov, A.L.1    Ravel, B.2    Conradson, S.D.3
  • 97
    • 84909614778 scopus 로고    scopus 로고
    • note
    • Reference deleted in proof.
  • 99
    • 0000424864 scopus 로고    scopus 로고
    • Theory of solid state contributions to the x-ray elastic scattering amplitude
    • Ankudinov, A. L., and J. J. Rehr. 2000. Theory of solid state contributions to the x-ray elastic scattering amplitude. Phys. Rev. B. 62:2437-2445.
    • (2000) Phys. Rev. B , vol.62 , pp. 2437-2445
    • Ankudinov, A.L.1    Rehr, J.J.2
  • 100
    • 0001555957 scopus 로고    scopus 로고
    • Multiple-scattering x-ray-absorption fine-structure Debye-Waller factor calculations
    • Poiarkova, A. V., and J. J. Rehr. 1999. Multiple-scattering x-ray-absorption fine-structure Debye-Waller factor calculations. Phys. Rev. B. 59:948-957.
    • (1999) Phys. Rev. B , vol.59 , pp. 948-957
    • Poiarkova, A.V.1    Rehr, J.J.2
  • 101
    • 11844260365 scopus 로고
    • High-order multiple-scattering calculations of x-ray-absorption fine structure
    • Rehr, J. J., R. C. Albers, and S. I. Zabinsky. 1992. High-order multiple-scattering calculations of x-ray-absorption fine structure. Phys. Rev. Lett. 69:3397-3400.
    • (1992) Phys. Rev. Lett. , vol.69 , pp. 3397-3400
    • Rehr, J.J.1    Albers, R.C.2    Zabinsky, S.I.3
  • 102
    • 0001661950 scopus 로고
    • Theoretical x-ray absorption fine structure standards
    • Rehr, J. J., J. Mustre de Leon, ..., R. C. Albers. 1991. Theoretical x-ray absorption fine structure standards. J. Am. Chem. Soc. 113: 5135-5140.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5135-5140
    • Rehr, J.J.1    Mustre De Leon, J.2    Albers, R.C.3
  • 103
    • 0018468080 scopus 로고
    • Ab initio calculations of amplitude and phase...X-ray absorption fine structure spectroscopy
    • Teo, B. K., and P. A. Lee. 1979. Ab initio calculations of amplitude and phase...x-ray absorption fine structure spectroscopy. J. Am. Chem. Soc. 101:2815-2832.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 2815-2832
    • Teo, B.K.1    Lee, P.A.2
  • 104
    • 35548993600 scopus 로고
    • A rapid, exact, curved-wave theory for EXAFS calculations
    • Gurnman, S. J., N. Binsted, and I. Ross. 1984. A rapid, exact, curved-wave theory for EXAFS calculations. J. Phys. C. 17:143-151.
    • (1984) J. Phys. C , vol.17 , pp. 143-151
    • Gurnman, S.J.1    Binsted, N.2    Ross, I.3


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