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Volumn 75, Issue 5, 2002, Pages 519-526

Photothermal monitoring of redox state of respiratory chain in single live cells

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C;

EID: 85047688714     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/0031-8655(2002)0750519PMORSO2.0.CO2     Document Type: Article
Times cited : (26)

References (58)
  • 2
    • 0023248892 scopus 로고
    • Intact organ spectrophotometry and single-photon counting
    • Sies, H. (1987) Intact organ spectrophotometry and single-photon counting. Arch. Toxicol. 60, 138-143.
    • (1987) Arch. Toxicol. , vol.60 , pp. 138-143
    • Sies, H.1
  • 3
    • 0000634122 scopus 로고
    • Red and far-red light action on oxidative phospohorylation
    • Gordon, S. A. and K. Surrey (1960) Red and far-red light action on oxidative phospohorylation. Radiat. Res. 12, 325-339.
    • (1960) Radiat. Res. , vol.12 , pp. 325-339
    • Gordon, S.A.1    Surrey, K.2
  • 4
    • 0022774474 scopus 로고
    • Studies of controlled reperfusion after Ischemia-III. Histochemical studies: Inability of triphenyltetrazolium chloride nonstaining to define tissue necrosis
    • Barnard, R. J. (1986) Studies of controlled reperfusion after Ischemia-III. Histochemical studies: inability of triphenyltetrazolium chloride nonstaining to define tissue necrosis J. Thorac. Cardiovasc. Surg. 92, 502-512.
    • (1986) J. Thorac. Cardiovasc. Surg. , vol.92 , pp. 502-512
    • Barnard, R.J.1
  • 7
    • 0011061089 scopus 로고
    • Fluorimetric studies of flavin component of the respiratory chain
    • (Edited by E. C. Slater). Elsevier, London
    • Chance, B. and B. Schoener (1966) Fluorimetric studies of flavin component of the respiratory chain. In Flavins and flavoproteins. (Edited by E. C. Slater), pp. 510-528. Elsevier, London.
    • (1966) Flavins and Flavoproteins , pp. 510-528
    • Chance, B.1    Schoener, B.2
  • 8
    • 0014470420 scopus 로고
    • Estimation of membrane potential and pH difference across the crystal membrane of rat liver mitochondria
    • Mitchell, P. and J. Moyle (1969) Estimation of membrane potential and pH difference across the crystal membrane of rat liver mitochondria. Eur. J. Biochem. 7, 471-484.
    • (1969) Eur. J. Biochem. , vol.7 , pp. 471-484
    • Mitchell, P.1    Moyle, J.2
  • 9
    • 0018665167 scopus 로고
    • Membrane potential of mitochondria measured with an electrode sensitive to tetraphenylphosphonium and relationship between proton electrochemical potential and phosphorylation potential state
    • Kamo N., M. Muratsugu, R. Hongoh and Y. Kobatake (1979) Membrane potential of mitochondria measured with an electrode sensitive to tetraphenylphosphonium and relationship between proton electrochemical potential and phosphorylation potential state. J. Membr. Biol. 49, 105-121.
    • (1979) J. Membr. Biol. , vol.49 , pp. 105-121
    • Kamo, N.1    Muratsugu, M.2    Hongoh, R.3    Kobatake, Y.4
  • 10
    • 0021207554 scopus 로고
    • Membrane potential and surface potential in mitochondria: Uptake and binding of lipophilic cations
    • Rottenberg, H. (1984) Membrane potential and surface potential in mitochondria: uptake and binding of lipophilic cations. J. Membr. Biol. 81, 3220-3226.
    • (1984) J. Membr. Biol. , vol.81 , pp. 3220-3226
    • Rottenberg, H.1
  • 11
    • 0034730139 scopus 로고    scopus 로고
    • Scanning electrochemical microscopy of living cells: Different redox activities of nonmetastatic and metastatic human breast cells
    • Liu, B., S. A. Rotenberg and M. V. Mirkin (2000) Scanning electrochemical microscopy of living cells: Different redox activities of nonmetastatic and metastatic human breast cells. Proc. Natl. Acad. Sci. USA. 97, 9855-9860.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9855-9860
    • Liu, B.1    Rotenberg, S.A.2    Mirkin, M.V.3
  • 14
    • 0023402228 scopus 로고
    • Videomicroscopic measurements in living cells: Dynamic determination of multiple end points for in vitro toxicology
    • Weiss, D. G. (1988) Videomicroscopic measurements in living cells: dynamic determination of multiple end points for in vitro toxicology. Mol. Toxicol. 1, 465-488.
    • (1988) Mol. Toxicol. , vol.1 , pp. 465-488
    • Weiss, D.G.1
  • 15
    • 0023402375 scopus 로고
    • New methods for cytotoxicity testing: Quantitative video microscopy of intracellular motion and mitochondria-specific fluorescence
    • Maile, W., T. Lindl and D. G. Weiss (1988) New methods for cytotoxicity testing: quantitative video microscopy of intracellular motion and mitochondria-specific fluorescence. Mol. Toxicol. 1, 427-437.
    • (1988) Mol. Toxicol. , vol.1 , pp. 427-437
    • Maile, W.1    Lindl, T.2    Weiss, D.G.3
  • 16
    • 0022438530 scopus 로고
    • Mitochondrial analysis in living cells: The use of rodamine 123 and flow cytometry
    • Ronot, X., L. Benel, M. Adolphe and J. C. Mounolou (1986) Mitochondrial analysis in living cells: the use of rodamine 123 and flow cytometry. Biol. Cell 57, 1-7.
    • (1986) Biol. Cell , vol.57 , pp. 1-7
    • Ronot, X.1    Benel, L.2    Adolphe, M.3    Mounolou, J.C.4
  • 19
    • 0025060816 scopus 로고
    • Inhibition and inactivation of NADH-cytochrome c reductase activity of bovine heart submitochondrial particles by the iron (III)-adriamycin complex
    • Hasinoff, B. B. (1990) Inhibition and inactivation of NADH-cytochrome c reductase activity of bovine heart submitochondrial particles by the iron (III)-adriamycin complex. Biochem. J. 265, 865-870.
    • (1990) Biochem. J. , vol.265 , pp. 865-870
    • Hasinoff, B.B.1
  • 20
    • 0030899962 scopus 로고    scopus 로고
    • Neuroleptic-induced mitochondrial enzyme alterations in the rat brain
    • Prince, J. A., M. S. Yassin and L. Oreland (1997) Neuroleptic-induced mitochondrial enzyme alterations in the rat brain. J. Pharmacol. Exp. Ther. 280, 261-267.
    • (1997) J. Pharmacol. Exp. Ther. , vol.280 , pp. 261-267
    • Prince, J.A.1    Yassin, M.S.2    Oreland, L.3
  • 21
    • 0030033035 scopus 로고    scopus 로고
    • Biochemical characterization of the effects of the benzodiazepine, midazolam, on mitochondrial electron transfer
    • Colleoni, M., B. Costa, E. Gori and A. Santagostino (1996) Biochemical characterization of the effects of the benzodiazepine, midazolam, on mitochondrial electron transfer. Pharmacol. Toxicol. 78, 69-76.
    • (1996) Pharmacol. Toxicol. , vol.78 , pp. 69-76
    • Colleoni, M.1    Costa, B.2    Gori, E.3    Santagostino, A.4
  • 23
    • 0033050168 scopus 로고    scopus 로고
    • Caffeine interaction with fluorescent calcium indicator dyes
    • Muschol, M., B. R. Dasgupta and B. M. Salzberg (1999) Caffeine interaction with fluorescent calcium indicator dyes. Biophys. J. 77, 577-586.
    • (1999) Biophys. J. , vol.77 , pp. 577-586
    • Muschol, M.1    Dasgupta, B.R.2    Salzberg, B.M.3
  • 24
    • 0025734172 scopus 로고
    • The effect of pH on rate constants, ion selectivity and thermodynamic properties of fluorescent calcium and magnesium indicators
    • Lattanzio, F. A. Jr. and D. K. Bartschat (1991) The effect of pH on rate constants, ion selectivity and thermodynamic properties of fluorescent calcium and magnesium indicators. Biochem. Biophys. Res. Commun. 177, 184-191.
    • (1991) Biochem. Biophys. Res. Commun. , vol.177 , pp. 184-191
    • Lattanzio F.A., Jr.1    Bartschat, D.K.2
  • 25
    • 0033543593 scopus 로고    scopus 로고
    • Advantages of calcium green-1 over other fluorescent dyes in measuring cytosolic calcium in platelets
    • Lee, S. K., J. Y. Lee, M. Y. Lee, S. M. Chung and J. H. Chung (1999) Advantages of calcium green-1 over other fluorescent dyes in measuring cytosolic calcium in platelets. Anal. Biochem. 273, 186-191.
    • (1999) Anal. Biochem. , vol.273 , pp. 186-191
    • Lee, S.K.1    Lee, J.Y.2    Lee, M.Y.3    Chung, S.M.4    Chung, J.H.5
  • 26
    • 0033163585 scopus 로고    scopus 로고
    • Errors caused by combination of Di-4 ANEPPS and Fluo3/4 for simultaneous measurements of transmembrane potentials and intracellular calcium
    • Johnson, P. L., W. Smith, T. C. Baynham and S. B. Knisley (1999) Errors caused by combination of Di-4 ANEPPS and Fluo3/4 for simultaneous measurements of transmembrane potentials and intracellular calcium. Ann. Biomed. Eng. 27, 563-571.
    • (1999) Ann. Biomed. Eng. , vol.27 , pp. 563-571
    • Johnson, P.L.1    Smith, W.2    Baynham, T.C.3    Knisley, S.B.4
  • 27
    • 85044700299 scopus 로고    scopus 로고
    • Evaluation of effect of the peptide structure on energetics of reduction-oxidation reactions of proteins containing Fe4S4 clusters in computer experiments
    • Ivaikina, A. G., N. K. Balabaev and K. V. Shaitan (2001) Evaluation of effect of the peptide structure on energetics of reduction-oxidation reactions of proteins containing Fe4S4 clusters in computer experiments. Biofizika 46, 589-594.
    • (2001) Biofizika , vol.46 , pp. 589-594
    • Ivaikina, A.G.1    Balabaev, N.K.2    Shaitan, K.V.3
  • 28
    • 0028049250 scopus 로고
    • Variable thermal emission and chlorophyll fluorescence in photosystem II particles
    • Allakhverdiev, S. I., V. V. Klimov and R. Carpentier (1994) Variable thermal emission and chlorophyll fluorescence in photosystem II particles. Proc. Natl. Acad. Sci. USA. 91, 281-285.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 281-285
    • Allakhverdiev, S.I.1    Klimov, V.V.2    Carpentier, R.3
  • 30
    • 0032573596 scopus 로고    scopus 로고
    • Demonstration of thermal dissipation of absorbed quanta during energy-dependent quenching of chlorophyll fluorescence in photosynthetic membranes
    • Yahyaoui, W., J. Harnois and R. Carpentier (1998) Demonstration of thermal dissipation of absorbed quanta during energy-dependent quenching of chlorophyll fluorescence in photosynthetic membranes. FEBS Lett. 440, 59-63.
    • (1998) FEBS Lett. , vol.440 , pp. 59-63
    • Yahyaoui, W.1    Harnois, J.2    Carpentier, R.3
  • 31
    • 0042910095 scopus 로고    scopus 로고
    • Unraveling photoexcited conformational changes of bacteriorhodopsin by time-resolved electron paramagnetic resonance spectroscopy
    • Rink, T., M. Pfeiffer, D. Oesterhelt, K. Gerwert and H. J. Steinhoff (2001) Unraveling photoexcited conformational changes of bacteriorhodopsin by time-resolved electron paramagnetic resonance spectroscopy. Biophys. J. 81, 1163-1170.
    • (2001) Biophys. J. , vol.81 , pp. 1163-1170
    • Rink, T.1    Pfeiffer, M.2    Oesterhelt, D.3    Gerwert, K.4    Steinhoff, H.J.5
  • 32
    • 0028331921 scopus 로고
    • Diffusivity of myoglobin in intact skeletal muscle cells
    • Jurgens, K. D., T. Peters and G. Gros (1994) Diffusivity of myoglobin in intact skeletal muscle cells. Proc. Natl. Acad. Sci. USA 91, 3829-3833.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3829-3833
    • Jurgens, K.D.1    Peters, T.2    Gros, G.3
  • 33
    • 0002004557 scopus 로고
    • Laser optoacoustic spectroscopy in chromatography
    • (Edited by V. S. Letokhov). Adam Hilger, Bristol and Boston
    • Zharov, V. P. (1989) Laser optoacoustic spectroscopy in chromatography. In Laser Analytical Spectrochemistry (Edited by V. S. Letokhov), pp. 229-271. Adam Hilger, Bristol and Boston.
    • (1989) Laser Analytical Spectrochemistry , pp. 229-271
    • Zharov, V.P.1
  • 34
    • 0001904672 scopus 로고
    • The theory of the photothermal effect in fluids
    • (Edited by J. Sell). Academic Press, Boston
    • Coupta, R. (1989) The theory of the photothermal effect in fluids. In Photothermals Investigation of Solids and Fluids (Edited by J. Sell), pp. 82-93. Academic Press, Boston.
    • (1989) Photothermals Investigation of Solids and Fluids , pp. 82-93
    • Coupta, R.1
  • 35
    • 0002197996 scopus 로고    scopus 로고
    • Overview of photothermal spectroscopy
    • (Edited by J. Sell). Academic Press, Boston
    • Tam, A. C. Overview of photothermal spectroscopy. In Photothermal Investigation of Solids and Fluids (Edited by J. Sell), pp. 1-34. Academic Press, Boston.
    • Photothermal Investigation of Solids and Fluids , pp. 1-34
    • Tam, A.C.1
  • 37
    • 0024297804 scopus 로고
    • Time-resolved photoacoustic calorimetry: Probing the energetics and dynamics of fast chemical and biochemical reactions
    • Peters, K. S. and G. J. Snyder (1988) Time-resolved photoacoustic calorimetry: probing the energetics and dynamics of fast chemical and biochemical reactions Science 241, 1053-1057.
    • (1988) Science , vol.241 , pp. 1053-1057
    • Peters, K.S.1    Snyder, G.J.2
  • 39
    • 0031049650 scopus 로고    scopus 로고
    • Photothermal beam deflection calorimetry in solution photochemistry: Recent progress and future prospects
    • Falvey, D. E. (1997) Photothermal beam deflection calorimetry in solution photochemistry: recent progress and future prospects. Photochem. Photobiol. 65, 4-9.
    • (1997) Photochem. Photobiol. , vol.65 , pp. 4-9
    • Falvey, D.E.1
  • 40
    • 0022727101 scopus 로고
    • Photoacoustic and photothermal methods applied to the study of radiationless deactivation processes in biological systems and in substances of biological interest
    • Braslavsky, S. E. (1986) Photoacoustic and photothermal methods applied to the study of radiationless deactivation processes in biological systems and in substances of biological interest. Photochem. Photobiol. 43, 667-675.
    • (1986) Photochem. Photobiol. , vol.43 , pp. 667-675
    • Braslavsky, S.E.1
  • 41
    • 0000601644 scopus 로고    scopus 로고
    • Selective destruction of protein function by chromophore-assisted laser inactivation
    • Jay, D. G. (1998) Selective destruction of protein function by chromophore-assisted laser inactivation. Proc. Natl. Acad. Sci. USA. 85, 5454-5458.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5454-5458
    • Jay, D.G.1
  • 42
    • 0027447640 scopus 로고
    • Biological effects of laser-induced shock waves: Structural and functional cell damage in vitro
    • Doukas, A. G., D. J. McAuliffe and T. J. Flotte (1993) Biological effects of laser-induced shock waves: structural and functional cell damage in vitro. Ultrasound Med. Biol. 19, 137-146.
    • (1993) Ultrasound Med. Biol. , vol.19 , pp. 137-146
    • Doukas, A.G.1    McAuliffe, D.J.2    Flotte, T.J.3
  • 44
    • 0002473798 scopus 로고
    • Rate process analysis of thermal damage
    • (Edited by A. J. Welch and M. J. C. Van Gemert). Plenum Press, New York
    • Pearce, J. and S. Thomsen (1995) Rate process analysis of thermal damage. In Optical-Thermal Response of Laser-Irradiated Tissue (Edited by A. J. Welch and M. J. C. Van Gemert), pp. 561-566. Plenum Press, New York.
    • (1995) Optical-Thermal Response of Laser-Irradiated Tissue , pp. 561-566
    • Pearce, J.1    Thomsen, S.2
  • 46
    • 0029453193 scopus 로고
    • Photothermal microscopy for cell imaging and diagnostics
    • Lapotko, D. and G. Kuchinsky (1995) Photothermal microscopy for cell imaging and diagnostics. J. Pro. SPIE Opt. Biophys. 2390, 89-100.
    • (1995) J. Pro. SPIE Opt. Biophys. , vol.2390 , pp. 89-100
    • Lapotko, D.1    Kuchinsky, G.2
  • 47
    • 0033707284 scopus 로고    scopus 로고
    • Functional imaging of single cells with photothermal microscopy
    • Lapotko, D. (2000) Functional imaging of single cells with photothermal microscopy. Proc. SPIE 3916, 268-277.
    • (2000) Proc. SPIE , vol.3916 , pp. 268-277
    • Lapotko, D.1
  • 48
    • 0011057477 scopus 로고    scopus 로고
    • Photothermal microscope
    • (Edited by F. Scudiery and M. Bertolotti). AIP, Rome
    • Lapotko, D. and G. Kuchinsky (1998) Photothermal microscope. In Photoacoustica and Photothermal Phenomena (Edited by F. Scudiery and M. Bertolotti), pp. 184-186. AIP, Rome.
    • (1998) Photoacoustica and Photothermal Phenomena , pp. 184-186
    • Lapotko, D.1    Kuchinsky, G.2
  • 49
    • 0001327023 scopus 로고
    • Electronic absorption spectra of hemes and hemoproteins
    • (Edited by D. Dolphin). Academic Press, New York
    • Adar, F. (1978) Electronic absorption spectra of hemes and hemoproteins. In The Porphyrins, Vol. III (Edited by D. Dolphin), pp. 167-182. Academic Press, New York.
    • (1978) The Porphyrins , vol.3 , pp. 167-182
    • Adar, F.1
  • 52
    • 0002312013 scopus 로고
    • Optical spectra and electronic structure of porphyrins and related rings
    • (Edited by D. Dolpin). Academic Press, New York
    • Gouterman, M. (1978) Optical spectra and electronic structure of porphyrins and related rings. In The Porphyrins, Vol. III (Edited by D. Dolpin), pp. 17-22. Academic Press, New York.
    • (1978) The Porphyrins , vol.3 , pp. 17-22
    • Gouterman, M.1
  • 55
    • 78651031094 scopus 로고
    • The respiratory chain and oxidative phosphorylation
    • Chance, B. and G. R. Williams (1956) The respiratory chain and oxidative phosphorylation. Adv. Enzymol. 17, 65-72.
    • (1956) Adv. Enzymol. , vol.17 , pp. 65-72
    • Chance, B.1    Williams, G.R.2
  • 56
    • 0011053742 scopus 로고
    • Localisation and assay of respiratory enzymes in living cells. Fluorescent nucleotide in aerobiosis and anaerobiosis
    • Chance, B. and B. Thorell (1960) Localisation and assay of respiratory enzymes in living cells. Fluorescent nucleotide in aerobiosis and anaerobiosis. Nature 194, 931-949.
    • (1960) Nature , vol.194 , pp. 931-949
    • Chance, B.1    Thorell, B.2
  • 57
    • 0033704890 scopus 로고    scopus 로고
    • Human cell viability to laser pulse and ion transport processes
    • Lapotko, D. and T. Romanovskaya (2000) Human cell viability to laser pulse and ion transport processes Proc. SPIE 3914, 262-269.
    • (2000) Proc. SPIE , vol.3914 , pp. 262-269
    • Lapotko, D.1    Romanovskaya, T.2
  • 58
    • 0034862618 scopus 로고    scopus 로고
    • Photothermal modification of optical microscope for noninvasive living cell monitoring
    • Lapotko, D., T. Romanovskaya and V. Zharov (2001) Photothermal modification of optical microscope for noninvasive living cell monitoring Proc. SPIE 4256, 43-52.
    • (2001) Proc. SPIE , vol.4256 , pp. 43-52
    • Lapotko, D.1    Romanovskaya, T.2    Zharov, V.3


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