메뉴 건너뛰기




Volumn 1607, Issue 2-3, 2003, Pages 191-202

Monitoring cytochrome redox changes in the mitochondria of intact cells using multi-wavelength visible light spectroscopy

Author keywords

Cellular respiration; Cytochrome redox state; Mitochondrial inhibitor; Nitric oxide; Visible light spectroscopy

Indexed keywords

ANTIMYCIN A1; CYTOCHROME; HALOGEN; MYXOTHIAZOL; NITRIC OXIDE; NITRIC OXIDE DONOR; OXYGEN; POTASSIUM CYANIDE; ROTENONE; TUNGSTEN;

EID: 0345490800     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2003.09.012     Document Type: Article
Times cited : (41)

References (45)
  • 2
    • 0030022592 scopus 로고    scopus 로고
    • The noninvasive measurement of absolute cerebral deoxyhemoglobin concentration and mean optical path length in the neonatal brain by second derivative near infrared spectroscopy
    • Cooper C.E., Elwell C.E., Meek J.H., Matcher S.J., Wyatt J.S., Cope M., Delpy D.T. The noninvasive measurement of absolute cerebral deoxyhemoglobin concentration and mean optical path length in the neonatal brain by second derivative near infrared spectroscopy. Pediatr. Res. 39:1996;32-38.
    • (1996) Pediatr. Res. , vol.39 , pp. 32-38
    • Cooper, C.E.1    Elwell, C.E.2    Meek, J.H.3    Matcher, S.J.4    Wyatt, J.S.5    Cope, M.6    Delpy, D.T.7
  • 3
    • 0026336993 scopus 로고
    • Skeletal muscle oxygenation monitoring by near infrared spectroscopy
    • De Blasi R.A., Quaglia E., Ferrari M. Skeletal muscle oxygenation monitoring by near infrared spectroscopy. Biochem. Int. 25:1991;241-248.
    • (1991) Biochem. Int. , vol.25 , pp. 241-248
    • De Blasi, R.A.1    Quaglia, E.2    Ferrari, M.3
  • 5
    • 0032494288 scopus 로고    scopus 로고
    • Oxidation and reduction of cytochrome oxidase in the neonatal brain observed by in vivo near-infrared spectroscopy
    • Quaresima V., Springett R., Cope M., Wyatt J.T., Delpy D.T., Ferrari M., Cooper C.E. Oxidation and reduction of cytochrome oxidase in the neonatal brain observed by in vivo near-infrared spectroscopy. Biochim. Biophys. Acta. 1366:1998;291-300.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 291-300
    • Quaresima, V.1    Springett, R.2    Cope, M.3    Wyatt, J.T.4    Delpy, D.T.5    Ferrari, M.6    Cooper, C.E.7
  • 7
    • 0029763762 scopus 로고    scopus 로고
    • Molecular oxygen modulates cytochrome c oxidase function
    • Chandel N.S., Budinger G.R., Schumacker P.T. Molecular oxygen modulates cytochrome c oxidase function. J. Biol. Chem. 271:1996;18672-18677.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18672-18677
    • Chandel, N.S.1    Budinger, G.R.2    Schumacker, P.T.3
  • 8
    • 0016397194 scopus 로고
    • Mitochondrial function under hypoxic conditions: The steady states of cytochrome alpha+alpha3 and their relation to mitochondrial energy states
    • Oshino N., Sugano T., Oshino R., Chance B. Mitochondrial function under hypoxic conditions: the steady states of cytochrome alpha+alpha3 and their relation to mitochondrial energy states. Biochim. Biophys. Acta. 368:1974;298-310.
    • (1974) Biochim. Biophys. Acta , vol.368 , pp. 298-310
    • Oshino, N.1    Sugano, T.2    Oshino, R.3    Chance, B.4
  • 9
    • 0023869404 scopus 로고
    • The oxygen dependence of mitochondrial oxidative phosphorylation measured by a new optical method for measuring oxygen concentration
    • Wilson D.F., Rumsey W.L., Green T.J., Vanderkooi J.M. The oxygen dependence of mitochondrial oxidative phosphorylation measured by a new optical method for measuring oxygen concentration. J. Biol. Chem. 263:1988;2712-2718.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2712-2718
    • Wilson, D.F.1    Rumsey, W.L.2    Green, T.J.3    Vanderkooi, J.M.4
  • 10
    • 0026064432 scopus 로고
    • Steady-state redox behavior of cytochrome c, cytochrome a, and CuA of cytochrome c oxidase in intact rat liver mitochondria
    • Morgan J.E., Wikstrom M. Steady-state redox behavior of cytochrome c, cytochrome a, and CuA of cytochrome c oxidase in intact rat liver mitochondria. Biochem. 30:1991;948-958.
    • (1991) Biochem. , vol.30 , pp. 948-958
    • Morgan, J.E.1    Wikstrom, M.2
  • 11
    • 0022461502 scopus 로고
    • Oxygen dependence of mitochondrial function in isolated rat cardiac myocytes
    • Kennedy F.G., Jones D.P. Oxygen dependence of mitochondrial function in isolated rat cardiac myocytes. Am. J. Physiol. 250:1986;C374-C383.
    • (1986) Am. J. Physiol. , vol.250
    • Kennedy, F.G.1    Jones, D.P.2
  • 12
    • 0024397557 scopus 로고
    • Mitochondrial function in normal and genetically altered cells and tissues
    • Chance B., Waterland R.A., Tanaka A., Poyton R.O. Mitochondrial function in normal and genetically altered cells and tissues. Ann. N. Y. Acad. Sci. 550:1988;360-373.
    • (1988) Ann. N. Y. Acad. Sci. , vol.550 , pp. 360-373
    • Chance, B.1    Waterland, R.A.2    Tanaka, A.3    Poyton, R.O.4
  • 13
    • 28044464985 scopus 로고
    • Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases
    • Cleeter M.W., Cooper J.M., Darley-Usmar V.M., Moncada S., Schapira A.H. Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases. FEBS Lett. 345:1994;50-54.
    • (1994) FEBS Lett. , vol.345 , pp. 50-54
    • Cleeter, M.W.1    Cooper, J.M.2    Darley-Usmar, V.M.3    Moncada, S.4    Schapira, A.H.5
  • 14
    • 0028134892 scopus 로고
    • Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase
    • Brown G.C., Cooper C.E. Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase. FEBS Lett. 356:1994;295-298.
    • (1994) FEBS Lett. , vol.356 , pp. 295-298
    • Brown, G.C.1    Cooper, C.E.2
  • 17
    • 0033573981 scopus 로고    scopus 로고
    • On the mechanism by which vascular endothelial cells regulate their oxygen consumption
    • Clementi E., Brown G.C., Foxwell N., Moncada S. On the mechanism by which vascular endothelial cells regulate their oxygen consumption. Proc. Natl. Acad. Sci. U. S. A. 96:1999;1559-1562.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 1559-1562
    • Clementi, E.1    Brown, G.C.2    Foxwell, N.3    Moncada, S.4
  • 20
    • 0015466489 scopus 로고
    • Compensation of measuring errors produced by finite response time in polarographic measurements with electrodes sensitive to oxygen and hydrogen
    • Wodick R. Compensation of measuring errors produced by finite response time in polarographic measurements with electrodes sensitive to oxygen and hydrogen. Pflügers Arch. 336:1972;327-344.
    • (1972) Pflügers Arch. , vol.336 , pp. 327-344
    • Wodick, R.1
  • 21
    • 0020420320 scopus 로고
    • Compensation for measuring error produced by finite response time in determination of rates of oxygen consumption with a Clark-type polarographic electrode
    • Ito S., Yamamoto T. Compensation for measuring error produced by finite response time in determination of rates of oxygen consumption with a Clark-type polarographic electrode. Anal. Biochem. 124:1982;440-445.
    • (1982) Anal. Biochem. , vol.124 , pp. 440-445
    • Ito, S.1    Yamamoto, T.2
  • 22
    • 0035155343 scopus 로고    scopus 로고
    • Bioenergetics at low oxygen: Dependence of respiration and phosphorylation on oxygen and adenosine diphosphate supply
    • Gnaiger E. Bioenergetics at low oxygen: dependence of respiration and phosphorylation on oxygen and adenosine diphosphate supply. Res. Physiol. 128:2001;277-297.
    • (2001) Res. Physiol. , vol.128 , pp. 277-297
    • Gnaiger, E.1
  • 23
    • 0028081969 scopus 로고
    • Use of the water absorption spectrum to quantify tissue chromophore concentration changes in near-infrared spectroscopy
    • Matcher S.J., Cope M., Delpy D.T. Use of the water absorption spectrum to quantify tissue chromophore concentration changes in near-infrared spectroscopy. Phys. Med. Biol. 38:1994;177-196.
    • (1994) Phys. Med. Biol. , vol.38 , pp. 177-196
    • Matcher, S.J.1    Cope, M.2    Delpy, D.T.3
  • 24
    • 0004147728 scopus 로고
    • Estimation of optical pathlength through tissue from direct time of flight measurement
    • Delpy D.T., Cope M., van der Zee P., Arridge S. Estimation of optical pathlength through tissue from direct time of flight measurement. Phys. Med. Biol. 248:1988;41-46.
    • (1988) Phys. Med. Biol. , vol.248 , pp. 41-46
    • Delpy, D.T.1    Cope, M.2    Van Der Zee, P.3    Arridge, S.4
  • 25
    • 0023832894 scopus 로고
    • Electron conduction between b cytochromes of the mitochondrial respiratory chain in the presence of antimycin plus myxothiazol
    • West I.C., Mitchell P., Rich P.R. Electron conduction between b cytochromes of the mitochondrial respiratory chain in the presence of antimycin plus myxothiazol. Biochim. Biophys. Acta. 933:1988;35-41.
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 35-41
    • West, I.C.1    Mitchell, P.2    Rich, P.R.3
  • 26
    • 0014958988 scopus 로고
    • Oxidation-reduction potentials of cytochromes in mitochondria
    • Dutton P.L., Wilson D.F., Lee C.P. Oxidation-reduction potentials of cytochromes in mitochondria. Biochem. 9:1970;5077-5082.
    • (1970) Biochem. , vol.9 , pp. 5077-5082
    • Dutton, P.L.1    Wilson, D.F.2    Lee, C.P.3
  • 28
    • 0026643964 scopus 로고
    • Detection of a near infra-red absorption band of ferrohaem a3 in cytochrome c oxidase
    • Rich P.R., Moody A.J., Ingledew A.J. Detection of a near infra-red absorption band of ferrohaem a3 in cytochrome c oxidase. FEBS Lett. 305:1992;171-173.
    • (1992) FEBS Lett. , vol.305 , pp. 171-173
    • Rich, P.R.1    Moody, A.J.2    Ingledew, A.J.3
  • 29
    • 0022839477 scopus 로고
    • A sensitive protein assay using microtiter plates
    • Sorensen K., Brodbeck U. A sensitive protein assay using microtiter plates. J. Immunol. Methods. 95:1986;291-293.
    • (1986) J. Immunol. Methods , vol.95 , pp. 291-293
    • Sorensen, K.1    Brodbeck, U.2
  • 30
    • 0009722636 scopus 로고
    • An introduction to the chemiosmotic theory
    • London: Academic Press
    • Nicholls D.G. An introduction to the chemiosmotic theory. Bioenergetics. 1982;Academic Press, London.
    • (1982) Bioenergetics
    • Nicholls, D.G.1
  • 31
    • 0032788156 scopus 로고    scopus 로고
    • Rapid and slow swelling during hypoxia in the CA1 region of rat hippocampal slices
    • Kreisman N.R., LaManna J.C. Rapid and slow swelling during hypoxia in the CA1 region of rat hippocampal slices. J. Neurophysiol. 82:1999;320-329.
    • (1999) J. Neurophysiol. , vol.82 , pp. 320-329
    • Kreisman, N.R.1    Lamanna, J.C.2
  • 33
    • 0025005012 scopus 로고
    • Cellular energetics and the oxygen dependence of respiration in cardiac myocytes isolated from adult rat
    • Rumsey W.L., Schlosser C., Nuutinen E.M., Robiolio M., Wilson D.F. Cellular energetics and the oxygen dependence of respiration in cardiac myocytes isolated from adult rat. J. Biol. Chem. 265:1990;15392-15399.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15392-15399
    • Rumsey, W.L.1    Schlosser, C.2    Nuutinen, E.M.3    Robiolio, M.4    Wilson, D.F.5
  • 34
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens J.F., Boveris A. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem. J. 191:1980;421-427.
    • (1980) Biochem. J. , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 36
    • 0030008040 scopus 로고    scopus 로고
    • Ubiquinol-cytochrome c oxidoreductase. The redox reactions of the bis-heme cytochrome b in ubiquinone-sufficient and ubiquinone-deficient systems
    • Matsuno-Yagi A., Hatefi Y. Ubiquinol-cytochrome c oxidoreductase. The redox reactions of the bis-heme cytochrome b in ubiquinone-sufficient and ubiquinone-deficient systems. J. Biol. Chem. 271:1996;6164-6171.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6164-6171
    • Matsuno-Yagi, A.1    Hatefi, Y.2
  • 38
    • 0029821342 scopus 로고    scopus 로고
    • NONOates (1-substituted diazen-1-ium-1,2-diolates) as nitric oxide donors: Convenient nitric oxide dosage forms
    • Keefer L.K., Nims R.W., Davies K.M., Wink D.A. NONOates (1-substituted diazen-1-ium-1,2-diolates) as nitric oxide donors: convenient nitric oxide dosage forms. Methods Enzymol. 268:1996;281-293.
    • (1996) Methods Enzymol. , vol.268 , pp. 281-293
    • Keefer, L.K.1    Nims, R.W.2    Davies, K.M.3    Wink, D.A.4
  • 39
    • 0030890094 scopus 로고    scopus 로고
    • Release of nitric oxide from donors with known half-life: A mathematical model for calculating nitric oxide concentrations in aerobic solutions
    • Schmidt K., Desch W., Klatt P., Kukovetz W.R., Mayer B. Release of nitric oxide from donors with known half-life: a mathematical model for calculating nitric oxide concentrations in aerobic solutions. Arch. Pharmacodyn. 355:1997;457-462.
    • (1997) Arch. Pharmacodyn. , vol.355 , pp. 457-462
    • Schmidt, K.1    Desch, W.2    Klatt, P.3    Kukovetz, W.R.4    Mayer, B.5
  • 41
    • 0024277361 scopus 로고
    • Early reduction of cytochrome c in hypoxia
    • Chance B. Early reduction of cytochrome c in hypoxia. FEBS Lett. 226:1988;343-346.
    • (1988) FEBS Lett. , vol.226 , pp. 343-346
    • Chance, B.1
  • 43
    • 0032321145 scopus 로고    scopus 로고
    • Mitochondrial respiration in the low oxygen environment of the cell. Effect of ADP on oxygen kinetics
    • Gnaiger E., Lassnig B., Kuznetsov A.V., Margreiter R. Mitochondrial respiration in the low oxygen environment of the cell. Effect of ADP on oxygen kinetics. Biochim. Biophys. Acta. 1365:1998;249-254.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 249-254
    • Gnaiger, E.1    Lassnig, B.2    Kuznetsov, A.V.3    Margreiter, R.4
  • 44
    • 0016681098 scopus 로고
    • Mitochondrial production of superoxide anions and its relationship to the antimycin insensitive respiration
    • Boveris A., Cadenas E. Mitochondrial production of superoxide anions and its relationship to the antimycin insensitive respiration. FEBS Lett. 54:1975;311-314.
    • (1975) FEBS Lett. , vol.54 , pp. 311-314
    • Boveris, A.1    Cadenas, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.