메뉴 건너뛰기




Volumn 1787, Issue 10, 2009, Pages 1276-1288

Inhibition of proton-transfer steps in transhydrogenase by transition metal ions

Author keywords

FTIR; Membrane protein; Proton translocation; Redox; Transhydrogenase; Zinc ion

Indexed keywords

ASPARTIC ACID; CADMIUM; COBALT; COPPER ION; GLUTAMIC ACID; HISTIDINE; LEAD; LYSINE; METAL ION; MUTANT PROTEIN; NICKEL; NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE; PROTON; ZINC ION;

EID: 67649976835     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2009.06.001     Document Type: Article
Times cited : (15)

References (91)
  • 1
    • 0030786197 scopus 로고    scopus 로고
    • Evidence that the transfer of hydride equivalents between nucleotides by proton-translocating transhydrogenase is direct
    • Venning J.D., Grimley R.L., Bizouarn T., Cotton N.P.J., and Jackson J.B. Evidence that the transfer of hydride equivalents between nucleotides by proton-translocating transhydrogenase is direct. J. Biol. Chem. 272 (1997) 27535-27538
    • (1997) J. Biol. Chem. , vol.272 , pp. 27535-27538
    • Venning, J.D.1    Grimley, R.L.2    Bizouarn, T.3    Cotton, N.P.J.4    Jackson, J.B.5
  • 2
    • 0013851517 scopus 로고
    • Stereochemistry of hydrogen transfer in the energy-linked pyridine nucleotide transhydrogenase and related reactions
    • Lee C.P., Simard-Duquesne N., Ernster L., and Hoberman H.D. Stereochemistry of hydrogen transfer in the energy-linked pyridine nucleotide transhydrogenase and related reactions. Biochim. Biophys. Acta 105 (1965) 397-409
    • (1965) Biochim. Biophys. Acta , vol.105 , pp. 397-409
    • Lee, C.P.1    Simard-Duquesne, N.2    Ernster, L.3    Hoberman, H.D.4
  • 3
    • 0023681148 scopus 로고
    • Physiological roles of nicotinamide nucleotide transhydrogenase
    • Rydstrom J., and Hoek J.B. Physiological roles of nicotinamide nucleotide transhydrogenase. Biochem. J. 254 (1988) 1-10
    • (1988) Biochem. J. , vol.254 , pp. 1-10
    • Rydstrom, J.1    Hoek, J.B.2
  • 4
    • 33745871211 scopus 로고    scopus 로고
    • Mitochondrial transhydrogenase-a key enzyme in insulin secretion and, potentially, diabetes.
    • Rydstrom J. Mitochondrial transhydrogenase-a key enzyme in insulin secretion and, potentially, diabetes. Trends Biochem. Sci. 31 (2006) 355-358
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 355-358
    • Rydstrom, J.1
  • 5
    • 0028048040 scopus 로고
    • Altered amino-acid metabolism in LRP mutants of Escherichia coli K12 and their derivatives
    • Ambartsoumian G., Dari R., Lin R.T., and Newman E.B. Altered amino-acid metabolism in LRP mutants of Escherichia coli K12 and their derivatives. Microbiology 140 (1994) 1737-1744
    • (1994) Microbiology , vol.140 , pp. 1737-1744
    • Ambartsoumian, G.1    Dari, R.2    Lin, R.T.3    Newman, E.B.4
  • 6
    • 0017335947 scopus 로고
    • Properties of glutathione release observed during reduction of organic hydroperoxide, demethylation of aminopyridineand oxidation of some substances in perfused rat liver, and their implications for the physiological function of catalase
    • Oshino N., and Chance B. Properties of glutathione release observed during reduction of organic hydroperoxide, demethylation of aminopyridineand oxidation of some substances in perfused rat liver, and their implications for the physiological function of catalase. Biochem. J. 162 (1977) 509-525
    • (1977) Biochem. J. , vol.162 , pp. 509-525
    • Oshino, N.1    Chance, B.2
  • 7
    • 18844415919 scopus 로고    scopus 로고
    • A Caenorhabditis elegans mutant lacking functional nicotinamide nucleotide transhydrogenase displays increased sensitivity to oxidative stress
    • Arkblad E.L., Tuck S., Pestov N.B., Dmitriev R.I., Kostina M.B., Stenvall J., Tranberg M., and Rydstrom J. A Caenorhabditis elegans mutant lacking functional nicotinamide nucleotide transhydrogenase displays increased sensitivity to oxidative stress. Free Radical Biol. Med. 38 (2005) 1518-1525
    • (2005) Free Radical Biol. Med. , vol.38 , pp. 1518-1525
    • Arkblad, E.L.1    Tuck, S.2    Pestov, N.B.3    Dmitriev, R.I.4    Kostina, M.B.5    Stenvall, J.6    Tranberg, M.7    Rydstrom, J.8
  • 8
    • 0036135679 scopus 로고    scopus 로고
    • A link between the membrane-bound pyridine nucleotide transhydrogenase and glutathione-dependent processes in Rhodobacter sphaeroides
    • Hickman J.W., Barber R.D., Skaar E.P., and Donohue T.J. A link between the membrane-bound pyridine nucleotide transhydrogenase and glutathione-dependent processes in Rhodobacter sphaeroides. J. Bact. 184 (2002) 400-409
    • (2002) J. Bact. , vol.184 , pp. 400-409
    • Hickman, J.W.1    Barber, R.D.2    Skaar, E.P.3    Donohue, T.J.4
  • 9
    • 0028339522 scopus 로고
    • Proton translocating transhydrogenase and NAD- and NADP-linked isocitrate dehydrogenases operate in a substrate cycle which contributes to the fine regulation of the tricarboxylic acid cycle activity in mitochondria
    • Sazanov L.A., and Jackson J.B. Proton translocating transhydrogenase and NAD- and NADP-linked isocitrate dehydrogenases operate in a substrate cycle which contributes to the fine regulation of the tricarboxylic acid cycle activity in mitochondria. FEBS Lett. 344 (1994) 109-116
    • (1994) FEBS Lett. , vol.344 , pp. 109-116
    • Sazanov, L.A.1    Jackson, J.B.2
  • 10
    • 33645088824 scopus 로고    scopus 로고
    • Nicotinamide nucleotide transhydrogenase: a key role in insulin secretion
    • Freeman H., Shimomura K., Horner E., Cox R.D., and Ashcroft F.M. Nicotinamide nucleotide transhydrogenase: a key role in insulin secretion. Cell. Metab. 3 (2006) 35-45
    • (2006) Cell. Metab. , vol.3 , pp. 35-45
    • Freeman, H.1    Shimomura, K.2    Horner, E.3    Cox, R.D.4    Ashcroft, F.M.5
  • 12
    • 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., and Baker P.J. Protein-protein recognition, hydride transfer and proton pumping in the transhydrogenase complex. Structure 8 (2000) 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
  • 14
    • 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., and Rydstrom J. X-ray structure of domain I of the proton-pumping membrane protein transhydrogenase from Escherichia coli. J. Mol. Biol. 352 (2005) 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
  • 16
    • 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.N.J., and Jackson J.B. The high resolution structure of the NADP(H)-binding component of proton-translocating transhydrogenase from human-heart mitochondria. Structure 8 (2000) 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.N.J.5    Jackson, J.B.6
  • 17
    • 0034663628 scopus 로고    scopus 로고
    • Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum
    • Jeeves M., Smith K.J., Quirk P.G., Cotton N.P.J., and Jackson J.B. Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum. Biochim. Biophys. Acta 1459 (2000) 248-257
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 248-257
    • Jeeves, M.1    Smith, K.J.2    Quirk, P.G.3    Cotton, N.P.J.4    Jackson, J.B.5
  • 18
    • 0035094747 scopus 로고    scopus 로고
    • The crystal structure of an asymmetric complex of the two nucleotide-binding components of proton-translocating transhydrogenase
    • Cotton N.P.J., White S.A., Peake S.J., McSweeney S., and Jackson J.B. The crystal structure of an asymmetric complex of the two nucleotide-binding components of proton-translocating transhydrogenase. Structure 9 (2001) 165-176
    • (2001) Structure , vol.9 , pp. 165-176
    • Cotton, N.P.J.1    White, S.A.2    Peake, S.J.3    McSweeney, S.4    Jackson, J.B.5
  • 19
    • 12544250957 scopus 로고    scopus 로고
    • Conformational diversity in NAD(H) and interacting transhydrogenase nicotinamide nucleotide binding domains
    • Sundaresan V., Chartron J., Yamaguchi M., and Stout C.D. Conformational diversity in NAD(H) and interacting transhydrogenase nicotinamide nucleotide binding domains. J. Mol. Biol. 346 (2005) 617-629
    • (2005) J. Mol. Biol. , vol.346 , pp. 617-629
    • Sundaresan, V.1    Chartron, J.2    Yamaguchi, M.3    Stout, C.D.4
  • 20
    • 4644229608 scopus 로고    scopus 로고
    • Active-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase
    • Mather O.M., van Boxel G.I., White S.A., and Jackson J.B. Active-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase. Biochemistry 43 (2004) 10952-10964
    • (2004) Biochemistry , vol.43 , pp. 10952-10964
    • Mather, O.M.1    van Boxel, G.I.2    White, S.A.3    Jackson, J.B.4
  • 21
    • 33947390415 scopus 로고    scopus 로고
    • Structures of the dI2dIII1 complex of proton-translocating transhydrogenase with bound, inactive analogues of NADH and NADPH revela active-site geometries
    • Bhakta T., Whitehead S.J., Snaith J.S., Dafforn T.R., Wilkie J., Rajesh S., White S.A., and Jackson J.B. Structures of the dI2dIII1 complex of proton-translocating transhydrogenase with bound, inactive analogues of NADH and NADPH revela active-site geometries. J. Biol. Chem. 46 (2007) 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
    • 0023857084 scopus 로고
    • The primary structure of the mitochondrial energy-linked nicotinamide nucleotide transhydrogenase deduced from the sequence ofcDNA clones
    • Yamaguchi M., Hatefi Y., Trach K., and Hoch J.A. The primary structure of the mitochondrial energy-linked nicotinamide nucleotide transhydrogenase deduced from the sequence ofcDNA clones. The Journal of Biological Chemistry 263 (1988) 2761-2767
    • (1988) The Journal of Biological Chemistry , vol.263 , pp. 2761-2767
    • Yamaguchi, M.1    Hatefi, Y.2    Trach, K.3    Hoch, J.A.4
  • 23
    • 0033516665 scopus 로고    scopus 로고
    • The membrane topology of proton-pumping Escherichia coli transhydrogenase determined by cysteine labelling
    • Meuller J., and Rydstrom J. The membrane topology of proton-pumping Escherichia coli transhydrogenase determined by cysteine labelling. J. Biol. Chem. 274 (1999) 19072-19080
    • (1999) J. Biol. Chem. , vol.274 , pp. 19072-19080
    • Meuller, J.1    Rydstrom, J.2
  • 24
    • 33646111905 scopus 로고    scopus 로고
    • A hybrid of the transhydrogenases from Rhodospirillum rubrum and Mycobacterium tuberculosis catalyses rapid hydride transfer but not the complete, proton-translocating reaction
    • Wilson R., Obiozo U.M., Quirk P.G., Besra G.D., and Jackson J.B. A hybrid of the transhydrogenases from Rhodospirillum rubrum and Mycobacterium tuberculosis catalyses rapid hydride transfer but not the complete, proton-translocating reaction. Biochim. Biophy. Acta 1537 (2006) 215-223
    • (2006) Biochim. Biophy. Acta , vol.1537 , pp. 215-223
    • Wilson, R.1    Obiozo, U.M.2    Quirk, P.G.3    Besra, G.D.4    Jackson, J.B.5
  • 25
    • 0037006970 scopus 로고    scopus 로고
    • The alternating site, binding change mechanism for proton translocation by transhydrogenase
    • Jackson J.B., White S.A., Quirk P.G., and Venning J.D. The alternating site, binding change mechanism for proton translocation by transhydrogenase. Biochemistry 41 (2002) 4173-4185
    • (2002) Biochemistry , vol.41 , pp. 4173-4185
    • Jackson, J.B.1    White, S.A.2    Quirk, P.G.3    Venning, J.D.4
  • 26
  • 27
    • 0034738090 scopus 로고    scopus 로고
    • Reverse engineering a protein: the mechanochemistry of ATP synthase
    • Oster G., and Wang H. Reverse engineering a protein: the mechanochemistry of ATP synthase. Biochim. Biophy. Acta 1458 (2000) 482-510
    • (2000) Biochim. Biophy. Acta , vol.1458 , pp. 482-510
    • Oster, G.1    Wang, H.2
  • 28
    • 0034866072 scopus 로고    scopus 로고
    • Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase angular torque profile of the enzyme
    • Panke O., Cherepanov A., Gumbiowski K., Engelbrecht E., and Junge W. Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase angular torque profile of the enzyme. Biophys. J. 81 (2001) 1220-1233
    • (2001) Biophys. J. , vol.81 , pp. 1220-1233
    • Panke, O.1    Cherepanov, A.2    Gumbiowski, K.3    Engelbrecht, E.4    Junge, W.5
  • 29
    • 0028114231 scopus 로고
    • Structure at 2.8A resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams J.P., Leslie A.G.W., Lutter R., and Walker J.E. Structure at 2.8A resolution of F1-ATPase from bovine heart mitochondria. Nature 370 (1994) 621-628
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.W.2    Lutter, R.3    Walker, J.E.4
  • 30
    • 0028361584 scopus 로고
    • Prediction and site-specific mutagenesis of residues in transmembrane alpha-helices of proton-pumping nicotinamide nucleotide transhydrogenases from Escherichia coli and bovine heart mitochondria
    • Holmberg E., Olausson T., Hultman T., Rydstrom J., Ahmad S., Glavas N.A., and Bragg P.D. Prediction and site-specific mutagenesis of residues in transmembrane alpha-helices of proton-pumping nicotinamide nucleotide transhydrogenases from Escherichia coli and bovine heart mitochondria. Biochemistry 33 (1994) 7691-7700
    • (1994) Biochemistry , vol.33 , pp. 7691-7700
    • Holmberg, E.1    Olausson, T.2    Hultman, T.3    Rydstrom, J.4    Ahmad, S.5    Glavas, N.A.6    Bragg, P.D.7
  • 31
    • 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., and Bragg P.D. Involvement of Histidine-91 of the beta subunit in proton translocation by the pyridine nucleotide transhydrogenase of Escherichia coli. Biochemistry 34 (1995) 7694-7702
    • (1995) Biochemistry , vol.34 , pp. 7694-7702
    • Glavas, N.A.1    Hou, C.2    Bragg, P.D.3
  • 32
    • 0029130956 scopus 로고
    • The mechanism of hydride transfer between 3-acetylpyridine adenine dinucleotide by the pyridine nucleotide transhydrogenase of Escherichia coli
    • Glavas N.A., and Bragg P.D. The mechanism of hydride transfer between 3-acetylpyridine adenine dinucleotide by the pyridine nucleotide transhydrogenase of Escherichia coli. Biochim. Biophys. Acta 1231 (1995) 297-303
    • (1995) Biochim. Biophys. Acta , vol.1231 , pp. 297-303
    • Glavas, N.A.1    Bragg, P.D.2
  • 33
    • 0029858086 scopus 로고    scopus 로고
    • The role of conserved histidine residues in the pyridine nucleotide transhydrogenase of Escherichia coli
    • Bragg P.D., and Hou C. The role of conserved histidine residues in the pyridine nucleotide transhydrogenase of Escherichia coli. Eur. J. Biochem. 241 (1996) 611-618
    • (1996) Eur. J. Biochem. , vol.241 , pp. 611-618
    • Bragg, P.D.1    Hou, C.2
  • 34
    • 0033514291 scopus 로고    scopus 로고
    • Site directed mutagenesis of charged and potentially proton carrying residues in the beta subunit of th eproton-translocating nicotinamide nucleotide transhydrogenase from Escherichia coli. Characterisation of beta H91, beta D392 and beta K424
    • Hu X., Zhang J.W., Fjellstrom O., Bizouarn T., and Rydstrom J. Site directed mutagenesis of charged and potentially proton carrying residues in the beta subunit of th eproton-translocating nicotinamide nucleotide transhydrogenase from Escherichia coli. Characterisation of beta H91, beta D392 and beta K424. Biochemistry 38 (1999) 1652-1658
    • (1999) Biochemistry , vol.38 , pp. 1652-1658
    • Hu, X.1    Zhang, J.W.2    Fjellstrom, O.3    Bizouarn, T.4    Rydstrom, J.5
  • 35
    • 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., and 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. 388 (2001) 299-307
    • (2001) Arch. Biochem. Biophys. , vol.388 , pp. 299-307
    • Bragg, P.D.1    Hou, C.2
  • 36
    • 0037072737 scopus 로고    scopus 로고
    • The proton channel of the energy-transducing nicotinamide nucleotide transhydrogenase of Escherichia coli
    • Yamaguchi M., Stout C.D., and Hatefi Y. The proton channel of the energy-transducing nicotinamide nucleotide transhydrogenase of Escherichia coli. J. Biol. Chem. 277 (2002) 33670-33675
    • (2002) J. Biol. Chem. , vol.277 , pp. 33670-33675
    • Yamaguchi, M.1    Stout, C.D.2    Hatefi, Y.3
  • 37
    • 0034652125 scopus 로고    scopus 로고
    • Determination of the binding sites of the proton transfer inhibitors Cd 2+ and Zn 2+ in bacterial reaction centres
    • Axelrod H.L., Abresch E.C., Paddock M.L., Okamura M.Y., and Feher G. Determination of the binding sites of the proton transfer inhibitors Cd 2+ and Zn 2+ in bacterial reaction centres. Proc. Nat. Acad. Sci. U. S. A. 97 (2000) 1542-1547
    • (2000) Proc. Nat. Acad. Sci. U. S. A. , vol.97 , pp. 1542-1547
    • Axelrod, H.L.1    Abresch, E.C.2    Paddock, M.L.3    Okamura, M.Y.4    Feher, G.5
  • 38
    • 0035852866 scopus 로고    scopus 로고
    • Retardation of proton transfer caused by binding of the transition metal ion to the bacterial reaction centre is due to pKa shifts of key protonatable residues
    • Gerencser L., and Maroti P. Retardation of proton transfer caused by binding of the transition metal ion to the bacterial reaction centre is due to pKa shifts of key protonatable residues. Biochemistry 40 (2001) 1850-1860
    • (2001) Biochemistry , vol.40 , pp. 1850-1860
    • Gerencser, L.1    Maroti, P.2
  • 39
    • 0037177829 scopus 로고    scopus 로고
    • Membrane potential-controlled inhibition of cytochrome c oxidase by Zinc
    • Mills D.A., Schmidt B., Hiser C., Westley E., and Ferguson-Miller S. Membrane potential-controlled inhibition of cytochrome c oxidase by Zinc. J. Biol. Chem. 277 (2002) 14894-14901
    • (2002) J. Biol. Chem. , vol.277 , pp. 14894-14901
    • Mills, D.A.1    Schmidt, B.2    Hiser, C.3    Westley, E.4    Ferguson-Miller, S.5
  • 40
    • 0037056044 scopus 로고    scopus 로고
    • Inhibition of proton transfer in cytochrome c oxidase by zinc ions: delayed proton uptake during oxygen reduction
    • Aagaard A., Namslauer A., and Brzezinski P. Inhibition of proton transfer in cytochrome c oxidase by zinc ions: delayed proton uptake during oxygen reduction. Biochim. Biophys. Acta 1555 (2002) 133-139
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 133-139
    • Aagaard, A.1    Namslauer, A.2    Brzezinski, P.3
  • 41
    • 0035903013 scopus 로고    scopus 로고
    • Zn 2+ binding to the cytoplasmic side of Paracoccus denitrificans cytochrome c oxidase selectively uncouples electron transfer and proton translocation
    • Kannt A., Ostermann T., Mueller H., and Ruitenberg M. Zn 2+ binding to the cytoplasmic side of Paracoccus denitrificans cytochrome c oxidase selectively uncouples electron transfer and proton translocation. FEBS Lett. 503 (2001) 142-146
    • (2001) FEBS Lett. , vol.503 , pp. 142-146
    • Kannt, A.1    Ostermann, T.2    Mueller, H.3    Ruitenberg, M.4
  • 42
    • 0028808109 scopus 로고
    • Zinc ions inhibit the QP centre of bovine heart mitochondrial bc1 complex by blocking a protonatable group
    • Link T.A., and Von Jagow G. Zinc ions inhibit the QP centre of bovine heart mitochondrial bc1 complex by blocking a protonatable group. J. Biol. Chem. 270 (1995) 25001-25006
    • (1995) J. Biol. Chem. , vol.270 , pp. 25001-25006
    • Link, T.A.1    Von Jagow, G.2
  • 43
    • 33845950074 scopus 로고    scopus 로고
    • The inhibition of mitochondrial complex I (NADH:ubiquinone oxidoreductase) by Zn2+
    • Sharpley M., and Hurst J. The inhibition of mitochondrial complex I (NADH:ubiquinone oxidoreductase) by Zn2+. J. Biol. Chem. 281 (2006) 34803-34809
    • (2006) J. Biol. Chem. , vol.281 , pp. 34803-34809
    • Sharpley, M.1    Hurst, J.2
  • 44
    • 0032763120 scopus 로고    scopus 로고
    • pH-dependent inhibition of voltage-gated H + currents in rat alveolar epithelial cells by Zn 2+ and other divalent cations
    • Cherny V.V., and DeCoursey T.E. pH-dependent inhibition of voltage-gated H + currents in rat alveolar epithelial cells by Zn 2+ and other divalent cations. J. Gen. Physiol. 114 (1999) 819-838
    • (1999) J. Gen. Physiol. , vol.114 , pp. 819-838
    • Cherny, V.V.1    DeCoursey, T.E.2
  • 46
    • 0034663688 scopus 로고    scopus 로고
    • Crystallographic location of two Zn 2+-binding sites in the avian cytochrome bc1 complex
    • Berry E.A., Zhang Z., Bellamy H.D., and Huang L. Crystallographic location of two Zn 2+-binding sites in the avian cytochrome bc1 complex. Biochim. Biophys. Acta 1459 (2000) 440-448
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 440-448
    • Berry, E.A.1    Zhang, Z.2    Bellamy, H.D.3    Huang, L.4
  • 51
    • 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.J.P., and Jackson J.B. Zinc ions selectively inhibit steps associated with binding and release of NADP(H) during turnover of proton-translocating transhydrogenase. FEBS Lett. 579 (2005) 2863-2867
    • (2005) FEBS Lett. , vol.579 , pp. 2863-2867
    • Whitehead, S.J.1    Rossington, K.E.2    Hafiz, A.3    Cotton, N.J.P.4    Jackson, J.B.5
  • 52
    • 0021879247 scopus 로고
    • Purification and properties of reconstitutively active nicotinamide nucleotide transhydrogenase of Escherichia coli
    • Clarke D.M., and Bragg P.D. Purification and properties of reconstitutively active nicotinamide nucleotide transhydrogenase of Escherichia coli. European Journal of Biochemistry 149 (1985) 517-523
    • (1985) European Journal of Biochemistry , vol.149 , pp. 517-523
    • Clarke, D.M.1    Bragg, P.D.2
  • 53
    • 0029671299 scopus 로고    scopus 로고
    • Estimation of the H+/H- ratio of the reaction catalysed by the nicotinamide nucleotide transhydrogenase in chromatophores from over-expressing strains of Rhodospirillum rubrumand in liposomes inlaid with the purified bovine enzyme
    • Bizouarn T., Sazanov L.A., Aubourg S., and Jackson J.B. Estimation of the H+/H- ratio of the reaction catalysed by the nicotinamide nucleotide transhydrogenase in chromatophores from over-expressing strains of Rhodospirillum rubrumand in liposomes inlaid with the purified bovine enzyme. Biochim. Biophys. Acta 1273 (1996) 4-12
    • (1996) Biochim. Biophys. Acta , vol.1273 , pp. 4-12
    • Bizouarn, T.1    Sazanov, L.A.2    Aubourg, S.3    Jackson, J.B.4
  • 54
    • 0028011867 scopus 로고
    • Kinetic resolution of the reaction catalysed by proton-translocating transhydrogenase from Escherichia coli as revealed by experiments with nucleotide substrate analogues
    • Hutton M.N., Day J.M., Bizouarn T., and Jackson J.B. Kinetic resolution of the reaction catalysed by proton-translocating transhydrogenase from Escherichia coli as revealed by experiments with nucleotide substrate analogues. Eur. J. Biochem. 219 (1994) 1041-1051
    • (1994) Eur. J. Biochem. , vol.219 , pp. 1041-1051
    • Hutton, M.N.1    Day, J.M.2    Bizouarn, T.3    Jackson, J.B.4
  • 55
    • 0030687619 scopus 로고    scopus 로고
    • The pH dependences of reactions catalysed by the complete proton-translocating transhydrogenase from Rhodosprillum rubrum, and by the complex formed from its recombinant peripheral, nucleotide-binding domains
    • Bizouarn T., Stilwell S.N., Venning J.M., Cotton N.P.J., and Jackson J.B. The pH dependences of reactions catalysed by the complete proton-translocating transhydrogenase from Rhodosprillum rubrum, and by the complex formed from its recombinant peripheral, nucleotide-binding domains. Biochim. Biophys. Acta 1322 (1997) 19-32
    • (1997) Biochim. Biophys. Acta , vol.1322 , pp. 19-32
    • Bizouarn, T.1    Stilwell, S.N.2    Venning, J.M.3    Cotton, N.P.J.4    Jackson, J.B.5
  • 56
    • 0026663910 scopus 로고
    • A mutation at Gly314 of the beta subunit of the Escherichia coli pyridine nucleotide transhydrogenase abolishes activity and affects the NADP(H)-induced conformational change
    • Ahmad S., Glavas N.A., and Bragg P.D. A mutation at Gly314 of the beta subunit of the Escherichia coli pyridine nucleotide transhydrogenase abolishes activity and affects the NADP(H)-induced conformational change. Eur. J. Biochem. 207 (1992) 733-739
    • (1992) Eur. J. Biochem. , vol.207 , pp. 733-739
    • Ahmad, S.1    Glavas, N.A.2    Bragg, P.D.3
  • 57
    • 33644645248 scopus 로고    scopus 로고
    • Molecular recognition between protein and nicotinamide dinucleotide in intact, proton-translocating transhydrogenase studied by ATR-FTIR spectroscopy
    • Iwaki M., Cotton N.J.P., Quirk P.G., Rich P.R., and Jackson J.B. Molecular recognition between protein and nicotinamide dinucleotide in intact, proton-translocating transhydrogenase studied by ATR-FTIR spectroscopy. J. Am. Chem. Soc. 128 (2006) 2621-2629
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 2621-2629
    • Iwaki, M.1    Cotton, N.J.P.2    Quirk, P.G.3    Rich, P.R.4    Jackson, J.B.5
  • 59
    • 0016657917 scopus 로고
    • Solubilization of membranes by detergents.
    • Helenius A., and Simons K. Solubilization of membranes by detergents. Biochim. Biophy. Acta 415 (1975) 29-79
    • (1975) Biochim. Biophy. Acta , vol.415 , pp. 29-79
    • Helenius, A.1    Simons, K.2
  • 61
    • 0026507657 scopus 로고
    • Nicotinamide nucleotide transhydrogenase from Rhodobacter capsulatus; the H+/H- ratio and the activation state of the enzyme during reduction of acetyl pyridine adenine dinucleotide
    • Palmer T., and Jackson J.B. Nicotinamide nucleotide transhydrogenase from Rhodobacter capsulatus; the H+/H- ratio and the activation state of the enzyme during reduction of acetyl pyridine adenine dinucleotide. Biochim. Biophys. Acta 1099 (1992) 157-162
    • (1992) Biochim. Biophys. Acta , vol.1099 , pp. 157-162
    • Palmer, T.1    Jackson, J.B.2
  • 62
    • 0029807116 scopus 로고    scopus 로고
    • Properties of the purified, recombinant, NADP(H)-binding domain III of the proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum
    • Diggle C., Bizouarn T., Cotton N.P.J., and Jackson J.B. Properties of the purified, recombinant, NADP(H)-binding domain III of the proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum. Eur. J. Biochem. 241 (1996) 162-170
    • (1996) Eur. J. Biochem. , vol.241 , pp. 162-170
    • Diggle, C.1    Bizouarn, T.2    Cotton, N.P.J.3    Jackson, J.B.4
  • 63
    • 0001730693 scopus 로고
    • Nicotinamide-adenine dinucleotides (NAD, NADP, NADH. NADPH): spectrophotometric and fluorometric methods.
    • Bergmeyer H.U. (Ed), Verlag Chemie, Weinheim
    • Klingenberg M. Nicotinamide-adenine dinucleotides (NAD, NADP, NADH. NADPH): spectrophotometric and fluorometric methods. In: Bergmeyer H.U. (Ed). Methods of Enzymatic Analysis 4 (1974), Verlag Chemie, Weinheim 2045-2072
    • (1974) Methods of Enzymatic Analysis , vol.4 , pp. 2045-2072
    • Klingenberg, M.1
  • 65
    • 0028905510 scopus 로고
    • The involvement of NADP(H) binding and release in energy transduction by proton-translocating nicotinamide nucleotide transhydrogenase from Escherichia coli
    • Bizouarn T., Grimley R.L., Cotton N.P.J., Stilwell S., Hutton M., and Jackson J.B. The involvement of NADP(H) binding and release in energy transduction by proton-translocating nicotinamide nucleotide transhydrogenase from Escherichia coli. Biochim. Biophys. Acta 1229 (1995) 49-58
    • (1995) Biochim. Biophys. Acta , vol.1229 , pp. 49-58
    • Bizouarn, T.1    Grimley, R.L.2    Cotton, N.P.J.3    Stilwell, S.4    Hutton, M.5    Jackson, J.B.6
  • 66
    • 0030904537 scopus 로고    scopus 로고
    • Effects of metal ions on the substrate-specificity of proton-pumping nicotinamide nucleotide transhydrogenase from Escherichia coli
    • Zhang J., Xiang H., Osman A.M., and Rydstrom J. Effects of metal ions on the substrate-specificity of proton-pumping nicotinamide nucleotide transhydrogenase from Escherichia coli. Biochim. Biophys. Acta 1319 (1997) 331-339
    • (1997) Biochim. Biophys. Acta , vol.1319 , pp. 331-339
    • Zhang, J.1    Xiang, H.2    Osman, A.M.3    Rydstrom, J.4
  • 67
    • 0030929158 scopus 로고    scopus 로고
    • The reduction of acetylpyridine adenine dinucleotide by NADH - is it a significant reaction of proton-translocating transhydrogenase, or an artefact
    • Stilwell S.N., Bizouarn T., and Jackson J.B. The reduction of acetylpyridine adenine dinucleotide by NADH - is it a significant reaction of proton-translocating transhydrogenase, or an artefact. Biochim. Biophys. Acta 1320 (1997) 83-94
    • (1997) Biochim. Biophys. Acta , vol.1320 , pp. 83-94
    • Stilwell, S.N.1    Bizouarn, T.2    Jackson, J.B.3
  • 68
    • 0038740878 scopus 로고    scopus 로고
    • Properties of the apo-form of the NADP(H)-binding domain III of proton-pumping Escherichia coli transhydrogense: implications for the reaction mechanism of the intact enzyme
    • Pedersen A., Karlsson J., Althage M., and Rydstrom J. Properties of the apo-form of the NADP(H)-binding domain III of proton-pumping Escherichia coli transhydrogense: implications for the reaction mechanism of the intact enzyme. Biochim. Biophys. Acta 1604 (2003) 55-59
    • (2003) Biochim. Biophys. Acta , vol.1604 , pp. 55-59
    • Pedersen, A.1    Karlsson, J.2    Althage, M.3    Rydstrom, J.4
  • 69
  • 70
    • 0037028562 scopus 로고    scopus 로고
    • Detection and imaging of zinc secretion from pancreatic beta-cells using a new fluorescent zinc indicator
    • Gee K.R., Zhou Z.L., Qian W.J., and Kennedy R. Detection and imaging of zinc secretion from pancreatic beta-cells using a new fluorescent zinc indicator. J. Am. Chem. Soc. 124 (2002) 776-778
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 776-778
    • Gee, K.R.1    Zhou, Z.L.2    Qian, W.J.3    Kennedy, R.4
  • 71
    • 34249706283 scopus 로고    scopus 로고
    • Methods to probe protein transitions with ATR infrared spectroscopy.
    • Rich P.R., and Iwaki M. Methods to probe protein transitions with ATR infrared spectroscopy. Mol. Biosyst. 3 (2007) 398-407
    • (2007) Mol. Biosyst. , vol.3 , pp. 398-407
    • Rich, P.R.1    Iwaki, M.2
  • 72
    • 0037061931 scopus 로고    scopus 로고
    • An initio density function theory calculations and vibrational analysis of zinc-bound 4-methylimidazol as a model of a histidine ligand in metalloenzymes
    • Hasegawa K., Ono T.-A., and Noguchi T. An initio density function theory calculations and vibrational analysis of zinc-bound 4-methylimidazol as a model of a histidine ligand in metalloenzymes. J. Phys. Chem. 106 (2002) 3377-3390
    • (2002) J. Phys. Chem. , vol.106 , pp. 3377-3390
    • Hasegawa, K.1    Ono, T.-A.2    Noguchi, T.3
  • 73
    • 0032464349 scopus 로고    scopus 로고
    • Analysis of zinc binding sites in protein crystal structures.
    • Alberts I.L., Nadassy K., and Wodak S.J. Analysis of zinc binding sites in protein crystal structures. Protein Science 7 (1998) 1700-1716
    • (1998) Protein Science , vol.7 , pp. 1700-1716
    • Alberts, I.L.1    Nadassy, K.2    Wodak, S.J.3
  • 74
    • 33644656189 scopus 로고    scopus 로고
    • Infrared protein spectroscopy as a tool to study protonation reactions within proteins.
    • Wikstrom M. (Ed), Royal Society of Chemsitry, Cambridge
    • Rich P.R., and Iwaki M. Infrared protein spectroscopy as a tool to study protonation reactions within proteins. In: Wikstrom M. (Ed). Biophysical and Structural Aspects of Bioenergetics (2005), Royal Society of Chemsitry, Cambridge 314-333
    • (2005) Biophysical and Structural Aspects of Bioenergetics , pp. 314-333
    • Rich, P.R.1    Iwaki, M.2
  • 75
    • 0034473318 scopus 로고    scopus 로고
    • The infrared absorption of amino acid side chains
    • Barth A. The infrared absorption of amino acid side chains. Prog. Biophys. Mol. Biol. 74 (2000) 141-173
    • (2000) Prog. Biophys. Mol. Biol. , vol.74 , pp. 141-173
    • Barth, A.1
  • 76
    • 0024102514 scopus 로고
    • Photoexcitation of rhodopsin: conformational changes in the chromophore, protein and associated lipids as determined by FTIR difference spectroscopy.
    • DeGrip W.J., Gray D., Gillespie J., Bovee P.H.M., Van den Berg E.M., Lugtenburg J., and Rothschild K.J. Photoexcitation of rhodopsin: conformational changes in the chromophore, protein and associated lipids as determined by FTIR difference spectroscopy. Photochem. Photobiol. 48 (1988) 497-504
    • (1988) Photochem. Photobiol. , vol.48 , pp. 497-504
    • DeGrip, W.J.1    Gray, D.2    Gillespie, J.3    Bovee, P.H.M.4    Van den Berg, E.M.5    Lugtenburg, J.6    Rothschild, K.J.7
  • 77
    • 0035928781 scopus 로고    scopus 로고
    • Identification of a region involved in the communication between the NADP(H)-binding domain and the membrane domain in proton pumping E. coli transhydrogenase
    • Althage M., Bizouarn T., and Rydstrom J. Identification of a region involved in the communication between the NADP(H)-binding domain and the membrane domain in proton pumping E. coli transhydrogenase. Biochemistry 40 (2001) 9968-9976
    • (2001) Biochemistry , vol.40 , pp. 9968-9976
    • Althage, M.1    Bizouarn, T.2    Rydstrom, J.3
  • 78
    • 0038053908 scopus 로고    scopus 로고
    • Proton translocation by transhydrogenase
    • Jackson J.B. Proton translocation by transhydrogenase. FEBS Lett. 545 (2003) 18-24
    • (2003) FEBS Lett. , vol.545 , pp. 18-24
    • Jackson, J.B.1
  • 79
    • 67649908390 scopus 로고    scopus 로고
    • Proton-translocating transhydrogenase in photosynthetic bacteria
    • Hunter C.N., Daldal F., Thurnauer M.C., and Beatty J.T. (Eds), Springer
    • Jackson J.B., and Obiozo U.M. Proton-translocating transhydrogenase in photosynthetic bacteria. In: Hunter C.N., Daldal F., Thurnauer M.C., and Beatty J.T. (Eds). The Purple Phototrophic Bacteria (2009), Springer 495-508
    • (2009) The Purple Phototrophic Bacteria , pp. 495-508
    • Jackson, J.B.1    Obiozo, U.M.2
  • 80
    • 0038728713 scopus 로고    scopus 로고
    • Roles of individual amino acid in helix 14 of the membrane domain of proton-translocating transhydrogensae from Escherichia coli as deduced from cysteine mutagenesis
    • Karlsson J., Althage M., and Rydstrom J. Roles of individual amino acid in helix 14 of the membrane domain of proton-translocating transhydrogensae from Escherichia coli as deduced from cysteine mutagenesis. Biochemistry 42 (2003) 6575-6581
    • (2003) Biochemistry , vol.42 , pp. 6575-6581
    • Karlsson, J.1    Althage, M.2    Rydstrom, J.3
  • 81
    • 0242664930 scopus 로고    scopus 로고
    • Essential glycine residues in the proton channel of Escherichia coli transhydrogenase
    • Yamaguchi M., and Stout C.D. Essential glycine residues in the proton channel of Escherichia coli transhydrogenase. J. Biol. Chem. 278 (2003) 45333-45339
    • (2003) J. Biol. Chem. , vol.278 , pp. 45333-45339
    • Yamaguchi, M.1    Stout, C.D.2
  • 82
    • 0032189631 scopus 로고    scopus 로고
    • Stopped-flow kinetics of hydride transfer between nucleotides by recombinant domains of proton-translocating transhydrogenase
    • Venning J.D., Bizouarn T., Cotton N.P.J., Quirk P.G., and Jackson J.B. Stopped-flow kinetics of hydride transfer between nucleotides by recombinant domains of proton-translocating transhydrogenase. Eur. J. Biochem. 257 (1998) 202-209
    • (1998) Eur. J. Biochem. , vol.257 , pp. 202-209
    • Venning, J.D.1    Bizouarn, T.2    Cotton, N.P.J.3    Quirk, P.G.4    Jackson, J.B.5
  • 83
    • 0035977025 scopus 로고    scopus 로고
    • Fast hydride transfer in proton-translocating transhydrogenase revealed in a rapid-mixing, continuous-flow device
    • Pinheiro T.J.T., Venning J.D., and Jackson J.B. Fast hydride transfer in proton-translocating transhydrogenase revealed in a rapid-mixing, continuous-flow device. J. Biol. Chem. 276 (2001) 44757-44761
    • (2001) J. Biol. Chem. , vol.276 , pp. 44757-44761
    • Pinheiro, T.J.T.1    Venning, J.D.2    Jackson, J.B.3
  • 84
    • 0030885668 scopus 로고    scopus 로고
    • Structural and catalytic properties of the expressed and purified NAD(H)- and NADP(H)-binding domains of proton-pumping transhydrogenase from Escherichia coli
    • Fjellstrom O., Johansson C., and Rydstrom J. Structural and catalytic properties of the expressed and purified NAD(H)- and NADP(H)-binding domains of proton-pumping transhydrogenase from Escherichia coli. Biochemistry 36 (1997) 11331-11341
    • (1997) Biochemistry , vol.36 , pp. 11331-11341
    • Fjellstrom, O.1    Johansson, C.2    Rydstrom, J.3
  • 85
    • 0035086791 scopus 로고    scopus 로고
    • A change in ionisation of the iolated NADP(H)-binding component (dIII) of transhydrogenase might be associated with the proton translocation pathway
    • Rodrigues D.J., Venning J.D., and Jackson J.B. A change in ionisation of the iolated NADP(H)-binding component (dIII) of transhydrogenase might be associated with the proton translocation pathway. Eur. J. Biochem. 268 (2001) 1430-1438
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1430-1438
    • Rodrigues, D.J.1    Venning, J.D.2    Jackson, J.B.3
  • 89
    • 50649111872 scopus 로고    scopus 로고
    • 2+-binding sites in proteins: implications with respect to toxicity
    • 2+-binding sites in proteins: implications with respect to toxicity. J. Inorganic Chem. 102 (2008) 1901-1909
    • (2008) J. Inorganic Chem. , vol.102 , pp. 1901-1909
    • Kirberger, M.1    Yang, J.Y.2
  • 90
    • 21744448180 scopus 로고    scopus 로고
    • Nucleotide binding affinities of the intact proton-translocating transhydrogenase from Escherichia coli
    • Bizouarn T., van Boxel G.I., Bhakta T., and Jackson J.B. Nucleotide binding affinities of the intact proton-translocating transhydrogenase from Escherichia coli. Biochim. Biophys. Acta 1708 (2005) 404-410
    • (2005) Biochim. Biophys. Acta , vol.1708 , pp. 404-410
    • Bizouarn, T.1    van Boxel, G.I.2    Bhakta, T.3    Jackson, J.B.4
  • 91
    • 0027370376 scopus 로고
    • GEPASI: a software package for modelling the dynamics, steady-state and control of biochemical and other systems
    • Mendes P. GEPASI: a software package for modelling the dynamics, steady-state and control of biochemical and other systems. Comput. Applic. Biosci. 9 (1993) 563-571
    • (1993) Comput. Applic. Biosci. , vol.9 , pp. 563-571
    • Mendes, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.