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Volumn 450, Issue , 2008, Pages 287-309

Chapter 14 Determination of Zinc Using Carbonic Anhydrase-Based Fluorescence Biosensors

Author keywords

[No Author keywords available]

Indexed keywords

CARBONATE DEHYDRATASE; ZINC;

EID: 58249091560     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(08)03414-9     Document Type: Review
Times cited : (31)

References (55)
  • 1
    • 0036557830 scopus 로고    scopus 로고
    • Preparation of metal ion buffers for biological experimentation: A methods approach with emphasis on iron and zinc
    • Aslamkhan A.G., Aslamkhan A., and Ahearn G.A. Preparation of metal ion buffers for biological experimentation: A methods approach with emphasis on iron and zinc. J. Exp. Zool. 292 (2002) 507-522
    • (2002) J. Exp. Zool. , vol.292 , pp. 507-522
    • Aslamkhan, A.G.1    Aslamkhan, A.2    Ahearn, G.A.3
  • 3
    • 0023674073 scopus 로고
    • Metal-buffered systems
    • Baker J.O. Metal-buffered systems. Methods Enzymol. 158 (1988) 33-55
    • (1988) Methods Enzymol. , vol.158 , pp. 33-55
    • Baker, J.O.1
  • 5
    • 33745029895 scopus 로고    scopus 로고
    • Measuring picomolar intracellular exchangeable zinc in PC-12 cells using a ratiometric fluorescence biosensor
    • Bozym R.A., Thompson R.B., Stoddard A.K., and Fierke C.A. Measuring picomolar intracellular exchangeable zinc in PC-12 cells using a ratiometric fluorescence biosensor. ACS Chem. Biol. 1 (2006) 103-111
    • (2006) ACS Chem. Biol. , vol.1 , pp. 103-111
    • Bozym, R.A.1    Thompson, R.B.2    Stoddard, A.K.3    Fierke, C.A.4
  • 6
    • 0014217558 scopus 로고
    • Combination of bovine carbonic anhydrase with a fluorescent sulfonamide
    • Chen R.F., and Kernohan J. Combination of bovine carbonic anhydrase with a fluorescent sulfonamide. J. Biol. Chem. 242 (1967) 5813-5823
    • (1967) J. Biol. Chem. , vol.242 , pp. 5813-5823
    • Chen, R.F.1    Kernohan, J.2
  • 7
    • 0000726701 scopus 로고    scopus 로고
    • Carbonic anhydrase-Evolution of the zinc binding site by nature and by design
    • Christianson D.W., and Fierke C.A. Carbonic anhydrase-Evolution of the zinc binding site by nature and by design. Acc. Chem. Res. 29 (1996) 331-339
    • (1996) Acc. Chem. Res. , vol.29 , pp. 331-339
    • Christianson, D.W.1    Fierke, C.A.2
  • 9
  • 10
    • 0025099503 scopus 로고
    • Mapping of fluorescence anisotropy in living cells by ratio imaging: Application to cytoplasmic viscosity
    • Dix J.A., and Verkman A.S. Mapping of fluorescence anisotropy in living cells by ratio imaging: Application to cytoplasmic viscosity. Biophys. J. 57 (1990) 231-240
    • (1990) Biophys. J. , vol.57 , pp. 231-240
    • Dix, J.A.1    Verkman, A.S.2
  • 11
    • 0030956737 scopus 로고    scopus 로고
    • Fluorescence methods for studying equilibrium macromolecule-Ligand interactions
    • Brand L., and Johnson M.L. (Eds), Academic Press, New York
    • Eftink M.R. Fluorescence methods for studying equilibrium macromolecule-Ligand interactions. In: Brand L., and Johnson M.L. (Eds). Fluorescence Spectroscopy Vol. 278 (1997), Academic Press, New York 221-257
    • (1997) Fluorescence Spectroscopy , vol.278 , pp. 221-257
    • Eftink, M.R.1
  • 12
    • 0029790057 scopus 로고    scopus 로고
    • Structure-based design of a sulfonamide probe for fluorescence anisotropy detection of zinc with a carbonic anhydrase-based biosensor
    • Elbaum D., Nair S.K., Patchan M.W., Thompson R.B., and Christianson D.W. Structure-based design of a sulfonamide probe for fluorescence anisotropy detection of zinc with a carbonic anhydrase-based biosensor. J. Am. Chem. Soc. 118 (1996) 8381-8387
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8381-8387
    • Elbaum, D.1    Nair, S.K.2    Patchan, M.W.3    Thompson, R.B.4    Christianson, D.W.5
  • 13
    • 0024218271 scopus 로고
    • Refined structure of human carbonic anhydrase II at 2.0A resolution
    • Eriksson A.E., and Jones T.A. Refined structure of human carbonic anhydrase II at 2.0A resolution. Proteins 4 (1988) 274-282
    • (1988) Proteins , vol.4 , pp. 274-282
    • Eriksson, A.E.1    Jones, T.A.2
  • 14
    • 0035693721 scopus 로고    scopus 로고
    • Fluorescence-based biosensing of zinc using carbonic anhydrase
    • Fierke C.A., and Thompson R.B. Fluorescence-based biosensing of zinc using carbonic anhydrase. BioMetals 14 (2001) 205-222
    • (2001) BioMetals , vol.14 , pp. 205-222
    • Fierke, C.A.1    Thompson, R.B.2
  • 15
    • 84981779372 scopus 로고
    • Intermolecular energy migration and fluorescence (Ger.)
    • Forster T. Intermolecular energy migration and fluorescence (Ger.). Ann. Phys. 2 (1948) 55-75
    • (1948) Ann. Phys. , vol.2 , pp. 55-75
    • Forster, T.1
  • 17
    • 0029989461 scopus 로고    scopus 로고
    • Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II
    • Huang C.-c., Lesburg C.A., Kiefer L.L., Fierke C.A., and Christianson D.W. Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II. Biochemistry 35 (1996) 3439-3446
    • (1996) Biochemistry , vol.35 , pp. 3439-3446
    • Huang, C.-c.1    Lesburg, C.A.2    Kiefer, L.L.3    Fierke, C.A.4    Christianson, D.W.5
  • 18
    • 0017393793 scopus 로고
    • A rapid and convenient preparation of apocarbonic anhydrase
    • Hunt J.B., Rhee M.J., and Storm C.B. A rapid and convenient preparation of apocarbonic anhydrase. Anal. Biochem. 79 (1977) 614-617
    • (1977) Anal. Biochem. , vol.79 , pp. 614-617
    • Hunt, J.B.1    Rhee, M.J.2    Storm, C.B.3
  • 19
    • 0033551442 scopus 로고    scopus 로고
    • Metal binding specificity in carbonic anhydrase is influenced by conserved hydrophobic amino acids
    • Hunt J.A., Ahmed M., and Fierke C.A. Metal binding specificity in carbonic anhydrase is influenced by conserved hydrophobic amino acids. Biochemistry 38 (1999) 9054-9060
    • (1999) Biochemistry , vol.38 , pp. 9054-9060
    • Hunt, J.A.1    Ahmed, M.2    Fierke, C.A.3
  • 21
    • 0028590042 scopus 로고
    • Functional characterization of human carbonic anhydrase II variants with altered zinc binding sites
    • Kiefer L.L., and Fierke C.A. Functional characterization of human carbonic anhydrase II variants with altered zinc binding sites. Biochemistry 33 (1994) 15233-15240
    • (1994) Biochemistry , vol.33 , pp. 15233-15240
    • Kiefer, L.L.1    Fierke, C.A.2
  • 22
    • 0028873117 scopus 로고
    • Hydrogen bond network in the metal binding site of carbonic anhydrase enhances zinc affinity and catalytic efficiency
    • Kiefer L.L., Paterno S.A., and Fierke C.A. Hydrogen bond network in the metal binding site of carbonic anhydrase enhances zinc affinity and catalytic efficiency. J. Am. Chem. Soc. 117 (1995) 6831-6837
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6831-6837
    • Kiefer, L.L.1    Paterno, S.A.2    Fierke, C.A.3
  • 23
    • 0031283056 scopus 로고    scopus 로고
    • Histidine to carboxamide ligand substitutions in the zinc binding site of carbonic anhydrase II alter metal coordination geometry but retain catalytic activity
    • Lesburg C.A., Huang C.-c., Christianson D.W., and Fierke C.A. Histidine to carboxamide ligand substitutions in the zinc binding site of carbonic anhydrase II alter metal coordination geometry but retain catalytic activity. Biochemistry 36 (1997) 15780-15791
    • (1997) Biochemistry , vol.36 , pp. 15780-15791
    • Lesburg, C.A.1    Huang, C.-c.2    Christianson, D.W.3    Fierke, C.A.4
  • 25
    • 0017370683 scopus 로고
    • Use of inhibitors in physiological studies of carbonic anhydrase
    • Maren T.H. Use of inhibitors in physiological studies of carbonic anhydrase. Am. J. Physiol. 232 (1977) F291-F297
    • (1977) Am. J. Physiol. , vol.232
    • Maren, T.H.1
  • 27
    • 1842591322 scopus 로고    scopus 로고
    • Probing determinants of the metal ion selectivity in carbonic anhydrase using mutagenesis
    • McCall K.A., and Fierke C.A. Probing determinants of the metal ion selectivity in carbonic anhydrase using mutagenesis. Biochemistry 43 (2004) 3979-3986
    • (2004) Biochemistry , vol.43 , pp. 3979-3986
    • McCall, K.A.1    Fierke, C.A.2
  • 28
    • 0031395452 scopus 로고    scopus 로고
    • Cu speciation and cyanobacterial distribution in harbors subject to anthropogenic Cu inputs
    • Moffett J.W., Brand L.E., Croot P.L., and Barbeau K.A. Cu speciation and cyanobacterial distribution in harbors subject to anthropogenic Cu inputs. Limnol. Oceanogr. 42 (1997) 789-799
    • (1997) Limnol. Oceanogr. , vol.42 , pp. 789-799
    • Moffett, J.W.1    Brand, L.E.2    Croot, P.L.3    Barbeau, K.A.4
  • 29
    • 28844435933 scopus 로고    scopus 로고
    • Qz1 and Qz2: Rapid, reversible quinoline-derivatized fluoresceins for sensing biological Zn(II)
    • Nolan E.M., Jaworski J., Okamoto K.-I., Hayashi Y., Sheng M., and Lippard S.J. Qz1 and Qz2: Rapid, reversible quinoline-derivatized fluoresceins for sensing biological Zn(II). J. Am. Chem. Soc. 127 (2005) 16812-16823
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 16812-16823
    • Nolan, E.M.1    Jaworski, J.2    Okamoto, K.-I.3    Hayashi, Y.4    Sheng, M.5    Lippard, S.J.6
  • 30
    • 0000373785 scopus 로고
    • A practical guide to the study of calcium in living cells
    • Wilson L., and Matsudaira P. (Eds), Academic Press, New York
    • Nuccitelli R. A practical guide to the study of calcium in living cells. In: Wilson L., and Matsudaira P. (Eds). Methods in Cell Biology Vol. 40 (1994), Academic Press, New York 364
    • (1994) Methods in Cell Biology , vol.40 , pp. 364
    • Nuccitelli, R.1
  • 31
    • 0012795129 scopus 로고    scopus 로고
    • Serum-free media for neural cell cultures
    • Federoff S., and Richardson A. (Eds), Humana Press, Totowa, NJ
    • Price P.J., and Brewer G.J. Serum-free media for neural cell cultures. In: Federoff S., and Richardson A. (Eds). Protocols for Neural Cell Culture (2001), Humana Press, Totowa, NJ 255-264
    • (2001) Protocols for Neural Cell Culture , pp. 255-264
    • Price, P.J.1    Brewer, G.J.2
  • 32
    • 0024383056 scopus 로고
    • A gene specifying subunit VIII of human cytochrome c oxidase is localized to chromosome 11 and is expressed in both muscle and non-muscle tissues
    • Rizzuto R., Nakase H., Darras B., Francke U., Fabrizi G.M., Mengel T., Walsh F., Kadenbach B., DiMauro S., and Schon E.A. A gene specifying subunit VIII of human cytochrome c oxidase is localized to chromosome 11 and is expressed in both muscle and non-muscle tissues. J. Biol. Chem. 264 (1989) 10595-10600
    • (1989) J. Biol. Chem. , vol.264 , pp. 10595-10600
    • Rizzuto, R.1    Nakase, H.2    Darras, B.3    Francke, U.4    Fabrizi, G.M.5    Mengel, T.6    Walsh, F.7    Kadenbach, B.8    DiMauro, S.9    Schon, E.A.10
  • 33
    • 0029311281 scopus 로고
    • Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells
    • Rizzuto R., Brini M., Pizzo P., Murgia M., and Pozzan T. Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells. Curr. Biol. 5 (1995) 635-642
    • (1995) Curr. Biol. , vol.5 , pp. 635-642
    • Rizzuto, R.1    Brini, M.2    Pizzo, P.3    Murgia, M.4    Pozzan, T.5
  • 34
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: Delivery of a biologically active protein into the mouse
    • Schwarze S.R., Ho A., Vocero-Akbani A., and Dowdy S.F. In vivo protein transduction: Delivery of a biologically active protein into the mouse. Science 285 (1999) 1569-1572
    • (1999) Science , vol.285 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 36
    • 0034018870 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors and their therapeutic potential
    • Supuran C.T., and Scozzafava A. Carbonic anhydrase inhibitors and their therapeutic potential. Exp. Opin. Ther. Patents 10 (2000) 575-600
    • (2000) Exp. Opin. Ther. Patents , vol.10 , pp. 575-600
    • Supuran, C.T.1    Scozzafava, A.2
  • 37
    • 0027225806 scopus 로고
    • Optical measurements of pH using fluorescence lifetimes and phase-modulation fluorometry
    • Szmacinski H., and Lakowicz J.R. Optical measurements of pH using fluorescence lifetimes and phase-modulation fluorometry. Anal. Chem. 65 (1993) 1668-1674
    • (1993) Anal. Chem. , vol.65 , pp. 1668-1674
    • Szmacinski, H.1    Lakowicz, J.R.2
  • 39
    • 0001356438 scopus 로고
    • Enzyme-based fiber optic zinc biosensor
    • Thompson R.B., and Jones E.R. Enzyme-based fiber optic zinc biosensor. Anal. Chem. 65 (1993) 730-734
    • (1993) Anal. Chem. , vol.65 , pp. 730-734
    • Thompson, R.B.1    Jones, E.R.2
  • 40
    • 0000762421 scopus 로고
    • Fluorescence lifetime-based biosensing of zinc: Origin of the broad dynamic range
    • Thompson R.B., and Patchan M.W. Fluorescence lifetime-based biosensing of zinc: Origin of the broad dynamic range. J. Fluorescence 5 (1995) 123-130
    • (1995) J. Fluorescence , vol.5 , pp. 123-130
    • Thompson, R.B.1    Patchan, M.W.2
  • 41
    • 0029069113 scopus 로고
    • Lifetime-based fluorescence energy transfer biosensing of zinc
    • Thompson R.B., and Patchan M.W. Lifetime-based fluorescence energy transfer biosensing of zinc. Anal. Biochem. 227 (1995) 123-128
    • (1995) Anal. Biochem. , vol.227 , pp. 123-128
    • Thompson, R.B.1    Patchan, M.W.2
  • 42
    • 0032533884 scopus 로고    scopus 로고
    • Determination of picomolar concentrations of metal ions using fluorescence anisotropy: Biosensing with a "reagentless" enzyme transducer
    • Thompson R.B., Maliwal B.P., Feliccia V.L., Fierke C.A., and McCall K. Determination of picomolar concentrations of metal ions using fluorescence anisotropy: Biosensing with a "reagentless" enzyme transducer. Anal. Chem. 70 (1998) 4717-4723
    • (1998) Anal. Chem. , vol.70 , pp. 4717-4723
    • Thompson, R.B.1    Maliwal, B.P.2    Feliccia, V.L.3    Fierke, C.A.4    McCall, K.5
  • 43
    • 0001606250 scopus 로고    scopus 로고
    • Expanded dynamic range of free zinc ion determination by fluorescence anisotropy
    • Thompson R.B., Maliwal B.P., and Fierke C.A. Expanded dynamic range of free zinc ion determination by fluorescence anisotropy. Anal. Chem. 70 (1998) 1749-1754
    • (1998) Anal. Chem. , vol.70 , pp. 1749-1754
    • Thompson, R.B.1    Maliwal, B.P.2    Fierke, C.A.3
  • 44
    • 0032691090 scopus 로고    scopus 로고
    • Fluorescence-based sensing of transition metal ions by a carbonic anhydrase transducer with a tethered fluorophore
    • Lakowicz J.R., Soper S.A., and Thompson R.B. (Eds), SPIE, Bellingham, WA
    • Thompson R.B., Maliwal B.P., and Fierke C.A. Fluorescence-based sensing of transition metal ions by a carbonic anhydrase transducer with a tethered fluorophore. In: Lakowicz J.R., Soper S.A., and Thompson R.B. (Eds). SPIE Conference on Advances in Fluorescence Sensing Technology IV Vol. 3602 (1999), SPIE, Bellingham, WA 85-92
    • (1999) SPIE Conference on Advances in Fluorescence Sensing Technology IV , vol.3602 , pp. 85-92
    • Thompson, R.B.1    Maliwal, B.P.2    Fierke, C.A.3
  • 45
    • 0034002451 scopus 로고    scopus 로고
    • Fluorescence microscopy of stimulated Zn(II) release from organotypic cultures of mammalian hippocampus using a carbonic anhydrase-based biosensor system
    • Thompson R.B., Whetsell Jr. W.O., Maliwal B.P., Fierke C.A., and Frederickson C.J. Fluorescence microscopy of stimulated Zn(II) release from organotypic cultures of mammalian hippocampus using a carbonic anhydrase-based biosensor system. J. Neurosci. Methods 96 (2000) 35-45
    • (2000) J. Neurosci. Methods , vol.96 , pp. 35-45
    • Thompson, R.B.1    Whetsell Jr., W.O.2    Maliwal, B.P.3    Fierke, C.A.4    Frederickson, C.J.5
  • 46
    • 0033624438 scopus 로고    scopus 로고
    • Zinc biosensing with multiphoton excitation using carbonic anhydrase and improved fluorophores
    • Thompson R.B., Maliwal B.P., and Zeng H.H. Zinc biosensing with multiphoton excitation using carbonic anhydrase and improved fluorophores. J. Biomed. Opt. 5 (2000) 17-22
    • (2000) J. Biomed. Opt. , vol.5 , pp. 17-22
    • Thompson, R.B.1    Maliwal, B.P.2    Zeng, H.H.3
  • 47
    • 0036816740 scopus 로고    scopus 로고
    • Excitation ratiometric fluorescent biosensor for zinc ion at picomolar levels
    • Thompson R.B., Cramer M.L., Bozym R., and Fierke C.A. Excitation ratiometric fluorescent biosensor for zinc ion at picomolar levels. J. Biomed. Opt. 7 (2002) 555-560
    • (2002) J. Biomed. Opt. , vol.7 , pp. 555-560
    • Thompson, R.B.1    Cramer, M.L.2    Bozym, R.3    Fierke, C.A.4
  • 50
    • 0021533503 scopus 로고
    • Determining the copper complexing capacity and conditional stability constants of complexes of copper (II) with natural organic ligands in seawater by cathodic stripping voltammetry of copper-catechol complex ions
    • van den Berg C. Determining the copper complexing capacity and conditional stability constants of complexes of copper (II) with natural organic ligands in seawater by cathodic stripping voltammetry of copper-catechol complex ions. Mar. Chem. 15 (1984) 1-18
    • (1984) Mar. Chem. , vol.15 , pp. 1-18
    • van den Berg, C.1
  • 51
    • 0000385283 scopus 로고
    • Photoelectric method for the measurement of the polarization of the fluorescence of solutions
    • Weber G. Photoelectric method for the measurement of the polarization of the fluorescence of solutions. J. Opt. Soc. Am. 46 (1956) 962-970
    • (1956) J. Opt. Soc. Am. , vol.46 , pp. 962-970
    • Weber, G.1
  • 53
    • 0346122959 scopus 로고    scopus 로고
    • Real-time determination of picomolar free Cu(II) in seawater using a fluorescence-based fiber optic biosensor
    • Zeng H.H., Thompson R.B., Maliwal B.P., Fones G.R., Moffett J.W., and Fierke C.A. Real-time determination of picomolar free Cu(II) in seawater using a fluorescence-based fiber optic biosensor. Anal. Chem. 75 (2003) 6807-6812
    • (2003) Anal. Chem. , vol.75 , pp. 6807-6812
    • Zeng, H.H.1    Thompson, R.B.2    Maliwal, B.P.3    Fones, G.R.4    Moffett, J.W.5    Fierke, C.A.6
  • 55
    • 84983853824 scopus 로고
    • A pH-dependent model for the chemical speciation of copper, zinc, cadmium, and lead in seawater
    • Zirino A., and Yamamoto S. A pH-dependent model for the chemical speciation of copper, zinc, cadmium, and lead in seawater. Limnol. Oceanogr. 17 (1972) 661-671
    • (1972) Limnol. Oceanogr. , vol.17 , pp. 661-671
    • Zirino, A.1    Yamamoto, S.2


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