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Volumn 1797, Issue 4, 2010, Pages 494-500

X-ray absorption studies of Zn2+-binding sites in Escherichia coli transhydrogenase and its ΒH91K mutant

Author keywords

Metal ion inhibition; Proton translocation; Transhydrogenase; XAFS; Zinc binding site

Indexed keywords

ASPARTIC ACID; GLUTAMIC ACID; HISTIDINE; LIGAND; LYSINE; NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE; PROTON; ZINC ION;

EID: 77049099541     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2010.01.006     Document Type: Article
Times cited : (6)

References (50)
  • 1
    • 0028808109 scopus 로고
    • Zinc ions inhibit the QP center of bovine heart mitochondrial bc1 complex by blocking a protonatable group
    • Link T.A., von Jagow G. Zinc ions inhibit the QP center of bovine heart mitochondrial bc1 complex by blocking a protonatable group. J. Biol. Chem. 1995, 270:25001-25006.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25001-25006
    • Link, T.A.1    von Jagow, G.2
  • 2
    • 33745607303 scopus 로고    scopus 로고
    • Inhibition of proton pumping by zinc ions during specific reaction steps in cytochrome c oxidase
    • Faxén K., Salomonsson L., Adelroth P., Brzezinski P. Inhibition of proton pumping by zinc ions during specific reaction steps in cytochrome c oxidase. Biochim. Biophys. Acta 2006, 1757:388-394.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 388-394
    • Faxén, K.1    Salomonsson, L.2    Adelroth, P.3    Brzezinski, P.4
  • 8
    • 0037085008 scopus 로고    scopus 로고
    • 2+ decelerates likewise the oxidation of cytochrome b, the reduction of cytochrome c1 and the voltage generation,
    • 2+ decelerates likewise the oxidation of cytochrome b, the reduction of cytochrome c1 and the voltage generation,. Biochim. Biophys. Acta 2002, 1553:177-182.
    • (2002) Biochim. Biophys. Acta , vol.1553 , pp. 177-182
    • Klishin, S.S.1    Junge, W.2    Mulkidjanian, A.Y.3
  • 13
    • 19444385817 scopus 로고    scopus 로고
    • Zinc ions selectively inhibit steps associated with binding and release of NADP(H) during turnover of proton-translocating transhydrogenase
    • Whitehead S.J., Rossington K.E., Hafiz A., Cotton N.P., Jackson J.B. Zinc ions selectively inhibit steps associated with binding and release of NADP(H) during turnover of proton-translocating transhydrogenase. FEBS Lett. 2005, 579:2863-2867.
    • (2005) FEBS Lett. , vol.579 , pp. 2863-2867
    • Whitehead, S.J.1    Rossington, K.E.2    Hafiz, A.3    Cotton, N.P.4    Jackson, J.B.5
  • 15
    • 0038053908 scopus 로고    scopus 로고
    • Proton translocation by transhydrogenase
    • Jackson J.B. Proton translocation by transhydrogenase. FEBS Lett. 2003, 545:18-24.
    • (2003) FEBS Lett. , vol.545 , pp. 18-24
    • Jackson, J.B.1
  • 16
    • 33644653670 scopus 로고    scopus 로고
    • Hydride transfer and proton translocation by nicotinamide nucleotide transhydrogenase
    • Royal Society of Chemistry, Cambridge, M. Wikstrom (Ed.)
    • Jackson J.B., White S.A., Brondijk T.H.C. Hydride transfer and proton translocation by nicotinamide nucleotide transhydrogenase. Biophysical and Structural Aspects of Bioenergetics 2005, 376-393. Royal Society of Chemistry, Cambridge. M. Wikstrom (Ed.).
    • (2005) Biophysical and Structural Aspects of Bioenergetics , pp. 376-393
    • Jackson, J.B.1    White, S.A.2    Brondijk, T.H.C.3
  • 17
    • 0034662750 scopus 로고    scopus 로고
    • Protein-protein recognition, hydride transfer and proton pumping in the transhydrogenase complex
    • Buckley P.A., Jackson J.B., Schneider T., White S.A., Rice D.W., Baker P.J. Protein-protein recognition, hydride transfer and proton pumping in the transhydrogenase complex. Structure 2000, 8:809-815.
    • (2000) Structure , vol.8 , pp. 809-815
    • Buckley, P.A.1    Jackson, J.B.2    Schneider, T.3    White, S.A.4    Rice, D.W.5    Baker, P.J.6
  • 18
    • 23944518970 scopus 로고    scopus 로고
    • X-ray structure of domain I of the proton-pumping membrane protein transhydrogenase from Escherichia coli
    • Johansson T., Oswald C., Pedersen A., Tornroth S., Okvist M., Karlsson B.G., Rydstrom J. X-ray structure of domain I of the proton-pumping membrane protein transhydrogenase from Escherichia coli. J. Mol. Biol. 2005, 352:299-312.
    • (2005) J. Mol. Biol. , vol.352 , pp. 299-312
    • Johansson, T.1    Oswald, C.2    Pedersen, A.3    Tornroth, S.4    Okvist, M.5    Karlsson, B.G.6    Rydstrom, J.7
  • 20
    • 0034650337 scopus 로고    scopus 로고
    • The high resolution structure of the NADP(H)-binding component of proton-translocating transhydrogenase from human-heart mitochondria
    • White S.A., Peake S.J., McSweeney S., Leonard G., Cotton N.P.J., Jackson J.B. The high resolution structure of the NADP(H)-binding component of proton-translocating transhydrogenase from human-heart mitochondria. Structure 2000, 8:1-12.
    • (2000) Structure , vol.8 , pp. 1-12
    • White, S.A.1    Peake, S.J.2    McSweeney, S.3    Leonard, G.4    Cotton, N.P.J.5    Jackson, J.B.6
  • 21
    • 33947390415 scopus 로고    scopus 로고
    • Structures of the dI2dIII1 complex of proton-translocating transhydrogenase with bound, inactive analogues of NADH and NADPH reveal active-site geometries
    • Bhakta T., Whitehead S.J., Snaith J.S., Dafforn T.R., Wilkie J., Rajesh S., White S.A., Jackson J.B. Structures of the dI2dIII1 complex of proton-translocating transhydrogenase with bound, inactive analogues of NADH and NADPH reveal active-site geometries. J. Biol. Chem. 2007, 46:3304-3318.
    • (2007) J. Biol. Chem. , vol.46 , pp. 3304-3318
    • Bhakta, T.1    Whitehead, S.J.2    Snaith, J.S.3    Dafforn, T.R.4    Wilkie, J.5    Rajesh, S.6    White, S.A.7    Jackson, J.B.8
  • 22
    • 0029047012 scopus 로고
    • Involvement of histidine-91 of the beta subunit in proton translocation by the pyridine nucleotide transhydrogenase of Escherichia coli
    • Glavas N.A., Hou C., Bragg P.D. Involvement of histidine-91 of the beta subunit in proton translocation by the pyridine nucleotide transhydrogenase of Escherichia coli. Biochemistry 1995, 34:7694-7702.
    • (1995) Biochemistry , vol.34 , pp. 7694-7702
    • Glavas, N.A.1    Hou, C.2    Bragg, P.D.3
  • 23
    • 0029130956 scopus 로고
    • The mechanism of hydride transfer between NADH and 3-acetyl pyridine adenine dinucleotide by the pyridine nucleotide transhydrogenase of Escherichia coli
    • Glavas N.A., Bragg P.D. The mechanism of hydride transfer between NADH and 3-acetyl pyridine adenine dinucleotide by the pyridine nucleotide transhydrogenase of Escherichia coli. Biochim. Biophys. Acta 1995, 1231:297-303.
    • (1995) Biochim. Biophys. Acta , vol.1231 , pp. 297-303
    • Glavas, N.A.1    Bragg, P.D.2
  • 24
    • 0029858086 scopus 로고    scopus 로고
    • The role of conserved histidine residues in the pyridine nucleotide transhydrogenase of Escherichia coli
    • Bragg P.D., Hou C. The role of conserved histidine residues in the pyridine nucleotide transhydrogenase of Escherichia coli. Eur. J. Biochem. 1996, 241:611-618.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 611-618
    • Bragg, P.D.1    Hou, C.2
  • 25
    • 0035870137 scopus 로고    scopus 로고
    • Characterisation of mutants of beta-histidine91, beta-aspartate213 and beta-asparagine222, possible components of the energy-transduction pathway of the proton-translocating pyridine nucleotide transhydrogenase of Escherichia coli
    • Bragg P.D., Hou C. Characterisation of mutants of beta-histidine91, beta-aspartate213 and beta-asparagine222, possible components of the energy-transduction pathway of the proton-translocating pyridine nucleotide transhydrogenase of Escherichia coli. Arch. Biochem. Biophys. 2001, 388:299-307.
    • (2001) Arch. Biochem. Biophys. , vol.388 , pp. 299-307
    • Bragg, P.D.1    Hou, C.2
  • 26
    • 0037072737 scopus 로고    scopus 로고
    • The proton channel of the energy-transducing nicotinamide nucleotide transhydrogenase of Escherichia coli
    • Yamaguchi M., Stout C.D., Hatefi Y. The proton channel of the energy-transducing nicotinamide nucleotide transhydrogenase of Escherichia coli. J. Biol. Chem. 2002, 277:33670-33675.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33670-33675
    • Yamaguchi, M.1    Stout, C.D.2    Hatefi, Y.3
  • 27
    • 0040631692 scopus 로고    scopus 로고
    • Structure of metal centres in proteins at subatomic resolution
    • Hasnain S.S., Hodgson K.O. Structure of metal centres in proteins at subatomic resolution. J. Synchr. Rad. 1999, 6:852-864.
    • (1999) J. Synchr. Rad. , vol.6 , pp. 852-864
    • Hasnain, S.S.1    Hodgson, K.O.2
  • 29
    • 77956993224 scopus 로고
    • Purification and assay of thermolysin
    • Academic Press, G.E. Perlmann, L. Lorand (Eds.)
    • Matsubara H. Purification and assay of thermolysin. Proteolytic Enzymes, vol.19 of Methods in Enzymology 1970, 642-651. Academic Press. G.E. Perlmann, L. Lorand (Eds.).
    • (1970) Proteolytic Enzymes, vol.19 of Methods in Enzymology , pp. 642-651
    • Matsubara, H.1
  • 32
    • 11844274669 scopus 로고    scopus 로고
    • Treatment of EXAFS data taken in fluorescence mode in non-linear conditions
    • Ciatto G., D'Acapito F., Boscherini F., Mobilio S. Treatment of EXAFS data taken in fluorescence mode in non-linear conditions. J. Synchr. Rad. 2004, 11:278-283.
    • (2004) J. Synchr. Rad. , vol.11 , pp. 278-283
    • Ciatto, G.1    D'Acapito, F.2    Boscherini, F.3    Mobilio, S.4
  • 33
    • 35949006418 scopus 로고
    • Near-edge X-ray-absorption fine structure of Pb: a comparison of theory and experiment
    • Newville M., Livins P., Yacoby Y., Rehr J.J., Stern E.A. Near-edge X-ray-absorption fine structure of Pb: a comparison of theory and experiment. Phys. Rev., B Condens. Matter 1993, 47:14126-14131.
    • (1993) Phys. Rev., B Condens. Matter , vol.47 , pp. 14126-14131
    • Newville, M.1    Livins, P.2    Yacoby, Y.3    Rehr, J.J.4    Stern, E.A.5
  • 34
    • 23844514184 scopus 로고    scopus 로고
    • ATHENA, ARTEMIS, HEPHAESTUS: data analysis for X-ray absorption spectroscopy using IFEFFIT
    • Ravel B., Newville M. ATHENA, ARTEMIS, HEPHAESTUS: data analysis for X-ray absorption spectroscopy using IFEFFIT. J. Synchr. Rad. 2005, 12:537-541.
    • (2005) J. Synchr. Rad. , vol.12 , pp. 537-541
    • Ravel, B.1    Newville, M.2
  • 35
    • 0034338303 scopus 로고    scopus 로고
    • Theoretical approaches to X-ray absorption fine structure
    • Rehr J.J., Albers R.C. Theoretical approaches to X-ray absorption fine structure. Rev. Mod. Phys. 2000, 72:621-654.
    • (2000) Rev. Mod. Phys. , vol.72 , pp. 621-654
    • Rehr, J.J.1    Albers, R.C.2
  • 36
    • 84942401063 scopus 로고
    • MOLDRAW: molecular graphics on a personal computer
    • Ugliengo P., Viterbo D., Chiari G. MOLDRAW: molecular graphics on a personal computer. Z. Kristallogr. 1993, 207:9.
    • (1993) Z. Kristallogr. , vol.207 , pp. 9
    • Ugliengo, P.1    Viterbo, D.2    Chiari, G.3
  • 37
    • 33744502092 scopus 로고    scopus 로고
    • Small revisions to predicted distances around metal sites in proteins
    • Harding M.M. Small revisions to predicted distances around metal sites in proteins. Acta Crystallogr., D Biol. Crystallogr. 2006, 62:678-682.
    • (2006) Acta Crystallogr., D Biol. Crystallogr. , vol.62 , pp. 678-682
    • Harding, M.M.1
  • 38
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Cryst. A 1991, 47:392-400.
    • (1991) Acta Cryst. A , vol.47 , pp. 392-400
    • Engh, R.1    Huber, R.2
  • 39
    • 12344305052 scopus 로고    scopus 로고
    • XAFS Debye-Waller factors for Zn metalloproteins
    • Dimakis N., Bunker G. XAFS Debye-Waller factors for Zn metalloproteins. Phys. Rev. B 2004, 70:195114.
    • (2004) Phys. Rev. B , vol.70 , pp. 195114
    • Dimakis, N.1    Bunker, G.2
  • 40
    • 0026620970 scopus 로고
    • Constrained and restrained refinement in EXAFS data analysis with curved wave theory
    • Binsted N., Strange R.W., Hasnain S.S. Constrained and restrained refinement in EXAFS data analysis with curved wave theory. Biochemistry 1992, 31:12117-12125.
    • (1992) Biochemistry , vol.31 , pp. 12117-12125
    • Binsted, N.1    Strange, R.W.2    Hasnain, S.S.3
  • 41
    • 0000260760 scopus 로고    scopus 로고
    • X-ray absorption near-edge structure calculations beyond the muffin-tin approximation
    • Joly Y. X-ray absorption near-edge structure calculations beyond the muffin-tin approximation. Phys. Rev. B 2001, 63:125120.
    • (2001) Phys. Rev. B , vol.63 , pp. 125120
    • Joly, Y.1
  • 42
    • 73449121405 scopus 로고    scopus 로고
    • Synergic approach to XAFS analysis for the identification of most probable binding motifs for mononuclear zinc sites in metalloproteins
    • Giachini L., Veronesi G., Francia F., Venturoli G., Boscherini F. Synergic approach to XAFS analysis for the identification of most probable binding motifs for mononuclear zinc sites in metalloproteins. J. Synchrotron. Radiat. 2010, 17. 10.1107/S090904950904919X.
    • (2010) J. Synchrotron. Radiat. , vol.17
    • Giachini, L.1    Veronesi, G.2    Francia, F.3    Venturoli, G.4    Boscherini, F.5
  • 44
    • 0032569167 scopus 로고    scopus 로고
    • The limitations of X-ray absorption spectroscopy for determining the structure of zinc sites in proteins. When is a tetrathiolate not a tetrathiolate?
    • Clark-Baldwin K., Tierney D.L., Govindaswamy N., Gruff E.S., Kim C., Berg J., Koch S.A., Penner-Hahn J.E. The limitations of X-ray absorption spectroscopy for determining the structure of zinc sites in proteins. When is a tetrathiolate not a tetrathiolate?. J. Am. Chem. Soc. 1998, 120:8401-8409.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8401-8409
    • Clark-Baldwin, K.1    Tierney, D.L.2    Govindaswamy, N.3    Gruff, E.S.4    Kim, C.5    Berg, J.6    Koch, S.A.7    Penner-Hahn, J.E.8
  • 45
    • 0032464349 scopus 로고    scopus 로고
    • Analysis of zinc binding sites in protein crystal structures
    • Alberts I.L., Nadassy K., Wodak S.J. Analysis of zinc binding sites in protein crystal structures. Protein Sci. 1998, 7:1700-1716.
    • (1998) Protein Sci. , vol.7 , pp. 1700-1716
    • Alberts, I.L.1    Nadassy, K.2    Wodak, S.J.3
  • 46
    • 0034129580 scopus 로고    scopus 로고
    • 3d EXAFS refinement of the Cu site of azurin sheds light on the nature of structural change at the metal centre in an oxidation-reduction process: an integrated approach combining EXAFS and crystallography
    • Cheung K.-C., Strange R.W., Hasnain S.S. 3d EXAFS refinement of the Cu site of azurin sheds light on the nature of structural change at the metal centre in an oxidation-reduction process: an integrated approach combining EXAFS and crystallography. Acta Crystallogr. D 2000, 56:697-704.
    • (2000) Acta Crystallogr. D , vol.56 , pp. 697-704
    • Cheung, K.-C.1    Strange, R.W.2    Hasnain, S.S.3
  • 47
    • 0020462668 scopus 로고
    • Structure of thermolysin refined at 1.6A resolution
    • Holmes M.A., Matthews B.W. Structure of thermolysin refined at 1.6A resolution. J. Mol. Biol. 1982, 160:623-639.
    • (1982) J. Mol. Biol. , vol.160 , pp. 623-639
    • Holmes, M.A.1    Matthews, B.W.2
  • 48
    • 0031569326 scopus 로고    scopus 로고
    • A critical assessment of the evidence from XAFS and crystallography for the breakage of the imidazolate bridge during catalysis in CuZn superoxide dismutase
    • Murphy L.M., Strange R.W., Hasnain S. A critical assessment of the evidence from XAFS and crystallography for the breakage of the imidazolate bridge during catalysis in CuZn superoxide dismutase. Structure 1997, 5:371-379.
    • (1997) Structure , vol.5 , pp. 371-379
    • Murphy, L.M.1    Strange, R.W.2    Hasnain, S.3
  • 49
    • 33846847704 scopus 로고    scopus 로고
    • Cytochrome c in a dry trehalose matrix: structural and dynamical effects probed by X-ray absorption spectroscopy
    • Giachini L., Francia F., Cordone L., Boscherini F., Venturoli G. Cytochrome c in a dry trehalose matrix: structural and dynamical effects probed by X-ray absorption spectroscopy. Biophys. J. 2007, 92:1350-1360.
    • (2007) Biophys. J. , vol.92 , pp. 1350-1360
    • Giachini, L.1    Francia, F.2    Cordone, L.3    Boscherini, F.4    Venturoli, G.5
  • 50
    • 0033516665 scopus 로고    scopus 로고
    • The membrane topology of proton-pumping Escherichia coli transhydrogenase determined by cysteine labelling
    • Meuller J., Rydstrom J. The membrane topology of proton-pumping Escherichia coli transhydrogenase determined by cysteine labelling. J. Biol. Chem. 1999, 274:19072-19080.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19072-19080
    • Meuller, J.1    Rydstrom, J.2


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