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Volumn 1, Issue 2, 2007, Pages 127-136

Characterizing multiple metal ion binding sites within a ribozyme by cadmium-induced EPR silencing

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EID: 85013257546     PISSN: 19552068     EISSN: 1955205X     Source Type: Journal    
DOI: 10.2976/1.2756332     Document Type: Article
Times cited : (33)

References (46)
  • 2
    • 0030931578 scopus 로고    scopus 로고
    • Calcium induces binding and formation of a spin-coupled dimanganese(II, II) center in the apowater oxidation complex of photosystem II as precursor to the functional tetra-Mn/Ca cluster
    • Ananyev, GM, and Dismukes, GC. 1997. “Calcium induces binding and formation of a spin-coupled dimanganese(II, II) center in the apowater oxidation complex of photosystem II as precursor to the functional tetra-Mn/Ca cluster.”. Biochemistry, 36:11342–11350.
    • (1997) Biochemistry , vol.36 , pp. 11342-11350
    • Ananyev, G.M.1    Dismukes, G.C.2
  • 3
    • 0023473840 scopus 로고
    • Electron paramagnetic resonance and magnetic susceptibility studies of dimanganese concanavalin A. Evidence for antiferromagnetic exchange coupling
    • Antanaitis, BC, Brown, RD, Chasteen, ND, Freedman, JH, Koenig, SH, Lilienthal, HR, Peisach, J, and Brewer, CF. 1987. “Electron paramagnetic resonance and magnetic susceptibility studies of dimanganese concanavalin A. Evidence for antiferromagnetic exchange coupling.”. Biochemistry, 26:7932–7937.
    • (1987) Biochemistry , vol.26 , pp. 7932-7937
    • Antanaitis, B.C.1    Brown, R.D.2    Chasteen, N.D.3    Freedman, J.H.4    Koenig, S.H.5    Lilienthal, H.R.6    Peisach, J.7    Brewer, C.F.8
  • 4
    • 33748559498 scopus 로고    scopus 로고
    • Nucleobase catalysis in ribozyme mechanism
    • Bevilacqua, PC, and Yajima, R. 2006. “Nucleobase catalysis in ribozyme mechanism.”. Curr. Opin. Chem. Biol., 10:455–464.
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 455-464
    • Bevilacqua, P.C.1    Yajima, R.2
  • 5
    • 0031055193 scopus 로고    scopus 로고
    • Manganese(II) active site mutants of 3,4-dihydroxyphenylacetate 2,3-dioxygenase fromArthrobacter globiformis strain CM-2
    • Boldt, YR, Whiting, AK, Wagner, ML, Sadowsky, MJ, Que, L, and Wackett, LP. 1997. “Manganese(II) active site mutants of 3,4-dihydroxyphenylacetate 2,3-dioxygenase fromArthrobacter globiformis strain CM-2.”. Biochemistry, 36:2147–2153.
    • (1997) Biochemistry , vol.36 , pp. 2147-2153
    • Boldt, Y.R.1    Whiting, A.K.2    Wagner, M.L.3    Sadowsky, M.J.4    Que, L.5    Wackett, L.P.6
  • 6
    • 33750985090 scopus 로고    scopus 로고
    • Pulse EPR methods for studying chemical and biological samples containing transition metals
    • Calle, C. 2006. “Pulse EPR methods for studying chemical and biological samples containing transition metals.”. Helv. Chim. Acta, 89:2495–2521.
    • (2006) Helv. Chim. Acta , vol.89 , pp. 2495-2521
    • Calle, C.1
  • 7
    • 0029113144 scopus 로고
    • Neomycin inhibition of the hammerhead ribozyme involves ionic interactions
    • Clouet-d'Orval, B, Stage, TK, and Uhlenbeck, OC. 1995. “Neomycin inhibition of the hammerhead ribozyme involves ionic interactions.”. Biochemistry, 34:11186–11190.
    • (1995) Biochemistry , vol.34 , pp. 11186-11190
    • Clouet-d'Orval, B.1    Stage, T.K.2    Uhlenbeck, O.C.3
  • 8
    • 19944427515 scopus 로고    scopus 로고
    • EPR and x-ray crystallographic characterization of the product-bound form of the MnII-loaded methionyl aminopeptidase from Pyrococcus furiosus
    • Copik, AJ, Nocek, BP, Swierczek, SI, Ruebush, S, Jang, SB, Meng, L, D'souza, VM, Peters, JW, Bennett, B, and Holz, RC. 2005. “EPR and x-ray crystallographic characterization of the product-bound form of the MnII-loaded methionyl aminopeptidase from Pyrococcus furiosus.”. Biochemistry, 44:121–129.
    • (2005) Biochemistry , vol.44 , pp. 121-129
    • Copik, A.J.1    Nocek, B.P.2    Swierczek, S.I.3    Ruebush, S.4    Jang, S.B.5    Meng, L.6    D'souza, V.M.7    Peters, J.W.8    Bennett, B.9    Holz, R.C.10
  • 9
    • 0036753229 scopus 로고    scopus 로고
    • Two decades of RNA catalysis
    • DeRose, V. 2002. “Two decades of RNA catalysis.”. Chem. Biol., 9:961–969.
    • (2002) Chem. Biol. , vol.9 , pp. 961-969
    • DeRose, V.1
  • 10
    • 0002495363 scopus 로고    scopus 로고
    • Distance measurements by cw and pulsed EPR
    • Berliner L.J., Eaton G.R., Eaton S.S., (eds), New York: Academic/Plenum
    • Eaton, SS, and Eaton, GR. 2000. “Distance measurements by cw and pulsed EPR.”. In Biological Magnetic Resonance, Edited by:Berliner, LJ, Eaton, GR, and Eaton, SS. 192–21. New York:Academic/Plenum.
    • (2000) Biological Magnetic Resonance , pp. 2-21
    • Eaton, S.S.1    Eaton, G.R.2
  • 11
    • 85024196500 scopus 로고    scopus 로고
    • 2+ EPR spectra. This document can be reached through a direct link in the online article's HTML reference section or via the EPAPS homepage (/pubservs/epaps.html)
    • 2+ EPR spectra. This document can be reached through a direct link in the online article's HTML reference section or via the EPAPS homepage (/pubservs/epaps.html). http://www.aip.org (http://www.aip.org)
  • 12
    • 20444472906 scopus 로고    scopus 로고
    • Multifrequency EPR analysis of the diamagnese cluster of the purivative sulfate thiohydrolase SoxB of Paracoccus pantotrophus
    • Epel, B, Schaefer, K-O, Quentmeier, A, Friedrich, C, and Lubitz, W. 2005. “Multifrequency EPR analysis of the diamagnese cluster of the purivative sulfate thiohydrolase SoxB of Paracoccus pantotrophus.”. J. Biol. Chem., 10:636–642.
    • (2005) J. Biol. Chem. , vol.10 , pp. 636-642
    • Epel, B.1    Schaefer, K.-O.2    Quentmeier, A.3    Friedrich, C.4    Lubitz, W.5
  • 13
    • 21244435487 scopus 로고    scopus 로고
    • Efficient preparation of organic substrate-RNA conjugates via in vitro transcription
    • Fiammengo, R, Musilek, K, and Jäschke, A. 2005. “Efficient preparation of organic substrate-RNA conjugates via in vitro transcription.”. J. Am. Chem. Soc., 127:9271–9276.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 9271-9276
    • Fiammengo, R.1    Musilek, K.2    Jäschke, A.3
  • 14
    • 34250613522 scopus 로고    scopus 로고
    • From nucleotides to ribozymes—a comparison of their metal ion binding properties
    • Freisinger, E, and Sigel, RKO. 2007. “From nucleotides to ribozymes—a comparison of their metal ion binding properties.”. Coord. Chem. Rev., 251:1834–1851.
    • (2007) Coord. Chem. Rev. , vol.251 , pp. 1834-1851
    • Freisinger, E.1    Sigel, R.K.O.2
  • 15
    • 0142075315 scopus 로고    scopus 로고
    • Quantitative analysis of dinuclear manganese(II) EPR spectra
    • Golombek, AP, and Hendrich, MP. 2003. “Quantitative analysis of dinuclear manganese(II) EPR spectra.”. J. Magn. Reson., 165:33–48.
    • (2003) J. Magn. Reson. , vol.165 , pp. 33-48
    • Golombek, A.P.1    Hendrich, M.P.2
  • 16
    • 36849103854 scopus 로고
    • 2+in glasses and compounds of the lithium borate system
    • 2+in glasses and compounds of the lithium borate system.”. J. Chem. Phys., 47:2711–2722.
    • (1967) J. Chem. Phys. , vol.47 , pp. 2711-2722
    • Griscom, D.L.1    Griscom, R.E.2
  • 17
    • 0026502537 scopus 로고
    • Multifrequency EPR investigations into the origin of the S2-state signal at g=4 of the O2-evolving complex
    • Haddy, A, Dunham, WR, Sands, RH, and Aasa, R. 1992. “Multifrequency EPR investigations into the origin of the S2-state signal at g=4 of the O2-evolving complex.”. Biochim. Biophys. Acta, 1099:25–34.
    • (1992) Biochim. Biophys. Acta , vol.1099 , pp. 25-34
    • Haddy, A.1    Dunham, W.R.2    Sands, R.H.3    Aasa, R.4
  • 18
    • 0032559057 scopus 로고    scopus 로고
    • Electron paramagnetic resonance spectroscopic measurement of Mn2+ binding affinities to the hammerhead ribozyme and correlation with cleavage activity
    • Horton, TE, Clardy, DR, and DeRose, VJ. 1998. “Electron paramagnetic resonance spectroscopic measurement of Mn2+ binding affinities to the hammerhead ribozyme and correlation with cleavage activity.”. Biochemistry, 37:18094–18101.
    • (1998) Biochemistry , vol.37 , pp. 18094-18101
    • Horton, T.E.1    Clardy, D.R.2    DeRose, V.J.3
  • 19
    • 4644305780 scopus 로고    scopus 로고
    • Architecture of a Diels-Alderase ribozyme with a preformed catalytic pocket
    • Keiper, S, Bebenroth, D, Seelig, B, Westhof, E, and Jäschke, A. 2004. “Architecture of a Diels-Alderase ribozyme with a preformed catalytic pocket.”. Chem. Biol., 11:1217–1227.
    • (2004) Chem. Biol. , vol.11 , pp. 1217-1227
    • Keiper, S.1    Bebenroth, D.2    Seelig, B.3    Westhof, E.4    Jäschke, A.5
  • 20
    • 0032499658 scopus 로고    scopus 로고
    • L-arginine binding to liver arginase requires proton transfer to gateway residue His141 and coordination of the guanidinium group to the dimanganese(II, II) center
    • Khangulov, SV. 1998. “L-arginine binding to liver arginase requires proton transfer to gateway residue His141 and coordination of the guanidinium group to the dimanganese(II, II) center.”. Biochemistry, 37:8539–8550.
    • (1998) Biochemistry , vol.37 , pp. 8539-8550
    • Khangulov, S.V.1
  • 21
    • 0028907382 scopus 로고
    • Determination of the metal ion separation and energies of the three lowest electronic states of dimanganese(II, II) complexes and enzymes: Catalase and liver arginase
    • Khangulov, SV, Pessiki, PJ, Barynin, VV, Ash, DE, and Dismukes, GC. 1995. “Determination of the metal ion separation and energies of the three lowest electronic states of dimanganese(II, II) complexes and enzymes:catalase and liver arginase.”. Biochemistry, 34:2015–2025.
    • (1995) Biochemistry , vol.34 , pp. 2015-2025
    • Khangulov, S.V.1    Pessiki, P.J.2    Barynin, V.V.3    Ash, D.E.4    Dismukes, G.C.5
  • 22
    • 11144342244 scopus 로고    scopus 로고
    • Binding of manganese(II) to a tertiary stabilized hammerhead ribozyme as studied by electron paramagnetic resonance spectroscopy
    • Kisseleva, N, Khvorova, A, Westhof, E, and Schiemann, O. 2005. “Binding of manganese(II) to a tertiary stabilized hammerhead ribozyme as studied by electron paramagnetic resonance spectroscopy.”. RNA, 11:1–6.
    • (2005) RNA , vol.11 , pp. 1-6
    • Kisseleva, N.1    Khvorova, A.2    Westhof, E.3    Schiemann, O.4
  • 24
    • 33845374771 scopus 로고
    • Manganese(II) complexes of polydentate Schiff bases. 1. Synthesis, characterization, magnetic properties, and molecular structure
    • Mabad, B, Cassoux, P, Tuchagues, J-P, and Hendrickson, DN. 1986. “Manganese(II) complexes of polydentate Schiff bases. 1. Synthesis, characterization, magnetic properties, and molecular structure.”. Inorg. Chem., 25:1420–1431.
    • (1986) Inorg. Chem. , vol.25 , pp. 1420-1431
    • Mabad, B.1    Cassoux, P.2    Tuchagues, J.-P.3    Hendrickson, D.N.4
  • 25
    • 33746228126 scopus 로고    scopus 로고
    • Tertiary contacts distant from the active site prime a ribozyme for catalysis
    • Martick, M, and Scott, WG. 2006. “Tertiary contacts distant from the active site prime a ribozyme for catalysis.”. Cell, 126:309–320.
    • (2006) Cell , vol.126 , pp. 309-320
    • Martick, M.1    Scott, W.G.2
  • 26
    • 0028063567 scopus 로고
    • Three-dimensional structure of a hammerhead ribozyme
    • Pley, HW, Flaherty, KM, and MacKay, DB. 1994. “Three-dimensional structure of a hammerhead ribozyme.”. Nature (London), 372:68–72.
    • (1994) Nature (London) , vol.372 , pp. 68-72
    • Pley, H.W.1    Flaherty, K.M.2    MacKay, D.B.3
  • 27
    • 26844515691 scopus 로고
    • EPR evidence for binuclear manganese(II) centers in rat liver arginase
    • Reczkowski, RS, and Ash, DE. 1992. “EPR evidence for binuclear manganese(II) centers in rat liver arginase.”. J. Am. Chem. Soc., 114:10992–10994.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10992-10994
    • Reczkowski, R.S.1    Ash, D.E.2
  • 28
    • 0015820471 scopus 로고
    • Electron paramagnetic studies of manganese(II)-pyruvate kinase-substrate complexes
    • Reed, GH, and Cohn, M. 1973. “Electron paramagnetic studies of manganese(II)-pyruvate kinase-substrate complexes.”. J. Biol. Chem., 248:6436–6442.
    • (1973) J. Biol. Chem. , vol.248 , pp. 6436-6442
    • Reed, G.H.1    Cohn, M.2
  • 29
    • 0002447550 scopus 로고
    • EPR of Mn(II) complexes with enzymes and other proteins
    • Reed, GH, and Markham, GD. 1984. “EPR of Mn(II) complexes with enzymes and other proteins.”. Biol. Magn. Reson., 6:73–142.
    • (1984) Biol. Magn. Reson. , vol.6 , pp. 73-142
    • Reed, G.H.1    Markham, G.D.2
  • 30
    • 85024234755 scopus 로고    scopus 로고
    • Siegel A., Siegel H., (eds), NewYork: Dekker
    • Reed, GH, and Poyner, RR. 2000. Metal Ions in Biological Systems, Edited by:Siegel, A., and Siegel, H., Vol. 37, 192–193. NewYork:Dekker.
    • (2000) Metal Ions in Biological Systems , vol.37 , pp. 192-193
    • Reed, G.H.1    Poyner, R.R.2
  • 32
    • 0142075321 scopus 로고    scopus 로고
    • 2+ binding site in the hammerhead ribozyme by EPR spectroscopy and DFT calculations. Effects of neomycin B on metal-ion binding
    • 2+ binding site in the hammerhead ribozyme by EPR spectroscopy and DFT calculations. Effects of neomycin B on metal-ion binding.”. ChemBioChem, 4:1057–1065.
    • (2003) ChemBioChem , vol.4 , pp. 1057-1065
    • Schiemann, O.1    Fritscher, J.2    Kisseleva, N.3    Sigurdsson, S.T.4    Prisner, T.F.5
  • 33
    • 0029073091 scopus 로고
    • The crystal structure of an all-RNA hammerhead ribozyme: A proposed mechanism for RNA catalytic cleavage
    • Scott, WG, Finch, JT, and Klug, A. 1995. “The crystal structure of an all-RNA hammerhead ribozyme:a proposed mechanism for RNA catalytic cleavage.”. Cell, 81:991–1002.
    • (1995) Cell , vol.81 , pp. 991-1002
    • Scott, W.G.1    Finch, J.T.2    Klug, A.3
  • 34
    • 0030476765 scopus 로고    scopus 로고
    • Capturing the structure of a catalytic RNA intermediate: The hammerhead ribozyme
    • Scott, WG, Murray, JB, Arnold, JRP, Stoddard, BL, and Klug, A. 1996. “Capturing the structure of a catalytic RNA intermediate:the hammerhead ribozyme.”. Science, 274:2065–2069.
    • (1996) Science , vol.274 , pp. 2065-2069
    • Scott, W.G.1    Murray, J.B.2    Arnold, J.R.P.3    Stoddard, B.L.4    Klug, A.5
  • 35
    • 0033102314 scopus 로고    scopus 로고
    • A small catalytic RNA motif with Diels-Alderase activity
    • Seelig, B, and Jäschke, A. 1999. “A small catalytic RNA motif with Diels-Alderase activity.”. Chem. Biol., 6:167–176.
    • (1999) Chem. Biol. , vol.6 , pp. 167-176
    • Seelig, B.1    Jäschke, A.2
  • 36
    • 0034671737 scopus 로고    scopus 로고
    • Enantioselective ribozyme catalysis of a bimolecular cycloaddition reaction
    • Seelig, B, Keiper, S, Stuhlmann, F, and Jäschke, A. 2000. “Enantioselective ribozyme catalysis of a bimolecular cycloaddition reaction.”. Angew. Chem., Int. Ed., 39:4576–4579.
    • (2000) Angew. Chem., Int. Ed. , vol.39 , pp. 4576-4579
    • Seelig, B.1    Keiper, S.2    Stuhlmann, F.3    Jäschke, A.4
  • 37
    • 20244375551 scopus 로고    scopus 로고
    • Structural basis for Diels-Alder ribozymecatalyzed carbon-carbon bond formation
    • Serganov, A. 2005. “Structural basis for Diels-Alder ribozymecatalyzed carbon-carbon bond formation.”. Nat. Struct. Mol. Biol., 12:218–224.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 218-224
    • Serganov, A.1
  • 38
    • 26944448948 scopus 로고    scopus 로고
    • Nucleoside 5-triphosphates: Selfassociation, acid-base, and metal ion-binding properties in solution
    • Sigel, H, and Griesser, R. 2005. “Nucleoside 5-triphosphates:selfassociation, acid-base, and metal ion-binding properties in solution.”. Chem. Soc. Rev., 34:875–900.
    • (2005) Chem. Soc. Rev. , vol.34 , pp. 875-900
    • Sigel, H.1    Griesser, R.2
  • 39
    • 33846887629 scopus 로고    scopus 로고
    • Alternative roles for metal ions in enzyme catalysis and the implications for ribozyme chemistry
    • Sigel, KO, and Pyle, AM. 2007. “Alternative roles for metal ions in enzyme catalysis and the implications for ribozyme chemistry.”. Chem. Rev. (Washington, D.C.), 107:97–113.
    • (2007) Chem. Rev. (Washington, D.C.) , vol.107 , pp. 97-113
    • Sigel, K.O.1    Pyle, A.M.2
  • 40
    • 0037012440 scopus 로고    scopus 로고
    • Characterization of an RNA active site: Interactions between a Diels-Alderase ribozyme and its substrates and products
    • Stuhlmann, F, and Jäschke, A. 2002. “Characterization of an RNA active site:interactions between a Diels-Alderase ribozyme and its substrates and products.”. J. Am. Chem. Soc., 124:3238–3244.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3238-3244
    • Stuhlmann, F.1    Jäschke, A.2
  • 43
    • 0035979330 scopus 로고    scopus 로고
    • Identification of the high affinity Mn2+ binding site of bacteriophage lambda phosphoprotein phosphatase: Effects of metal ligand mutations on electron paramagnetic resonance spectra and phosphatase activities
    • White, DJ, Reiter, NJ, Sikkink, RA, Yu, L, and Rusnak, F. 2001. “Identification of the high affinity Mn2+ binding site of bacteriophage lambda phosphoprotein phosphatase:effects of metal ligand mutations on electron paramagnetic resonance spectra and phosphatase activities.”. Biochemistry, 40:8918–8929.
    • (2001) Biochemistry , vol.40 , pp. 8918-8929
    • White, D.J.1    Reiter, N.J.2    Sikkink, R.A.3    Yu, L.4    Rusnak, F.5
  • 44
    • 0001127922 scopus 로고
    • Active site spectral studies on manganese superoxide dismutase
    • Whittaker, JW, and Whittaker, MM. 1991. “Active site spectral studies on manganese superoxide dismutase.”. J. Am. Chem. Soc., 113:5528–5540.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5528-5540
    • Whittaker, J.W.1    Whittaker, M.M.2
  • 46
    • 33846595826 scopus 로고    scopus 로고
    • Diels-Alder ribozyme catalysis: A computational approach
    • Zhang, X, and Bruice, TC. 2007. “Diels-Alder ribozyme catalysis:a computational approach.”. J. Am. Chem. Soc., 129:1001–1007.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 1001-1007
    • Zhang, X.1    Bruice, T.C.2


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