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Volumn 456, Issue A, 2009, Pages 267-285

Chapter 15 Isolation of Saccharomyces Cerevisiae Mitochondria for Mössbauer, Epr, and Electronic Absorption Spectroscopic Analyses

Author keywords

[No Author keywords available]

Indexed keywords

IRON SULFUR PROTEIN; OXYGEN;

EID: 63449089627     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(08)04415-7     Document Type: Review
Times cited : (21)

References (27)
  • 1
    • 0034636795 scopus 로고    scopus 로고
    • IscU as a scaffold for iron-sulfur cluster biosynthesis: Sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU
    • Agar J.N., Krebs C., Frazzon J., Huynh B.H., Dean D.R., and Johnson M.K. IscU as a scaffold for iron-sulfur cluster biosynthesis: Sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU. Biochemistry 39 (2000) 7856-7862
    • (2000) Biochemistry , vol.39 , pp. 7856-7862
    • Agar, J.N.1    Krebs, C.2    Frazzon, J.3    Huynh, B.H.4    Dean, D.R.5    Johnson, M.K.6
  • 2
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging review
    • Balaban R.S., and Nemoto S. Mitochondria, oxidants, and aging review. Cell 120 (2005) 483-495
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2
  • 3
    • 0037122943 scopus 로고    scopus 로고
    • Spectroscopy of succinate dehydrogenase, a historical perspective
    • Beinert H. Spectroscopy of succinate dehydrogenase, a historical perspective. Biochim. Biophys. Acta 1553 (2002) 7-22
    • (2002) Biochim. Biophys. Acta , vol.1553 , pp. 7-22
    • Beinert, H.1
  • 4
    • 0000654355 scopus 로고
    • Simple and rapid assay of oxidative phosphorylation
    • Chance B., and Willams G.R. Simple and rapid assay of oxidative phosphorylation. Nature 175 (1955) 1120-1121
    • (1955) Nature , vol.175 , pp. 1120-1121
    • Chance, B.1    Willams, G.R.2
  • 5
    • 0035235373 scopus 로고    scopus 로고
    • Isolation and subfractionation of mitochondria from the yeast Saccharomyces cerevisiae
    • Diekert K., deKroon A.I.P.M., Kispal G., and Lill R. Isolation and subfractionation of mitochondria from the yeast Saccharomyces cerevisiae. Methods Cell Biol. 65 (2001) 37-51
    • (2001) Methods Cell Biol. , vol.65 , pp. 37-51
    • Diekert, K.1    deKroon, A.I.P.M.2    Kispal, G.3    Lill, R.4
  • 6
    • 0028800976 scopus 로고
    • Isolation of highly purified mitochondria from Saccharomyces cerevisiae
    • Glick B.S., and Pon L.A. Isolation of highly purified mitochondria from Saccharomyces cerevisiae. Methods Enzymol. 260 (1995) 213-223
    • (1995) Methods Enzymol. , vol.260 , pp. 213-223
    • Glick, B.S.1    Pon, L.A.2
  • 7
    • 0021735773 scopus 로고
    • Ferrous ion-EDTA-stimulated phospholipid peroxidation
    • Gutteridge J.M.C. Ferrous ion-EDTA-stimulated phospholipid peroxidation. Biochem. J 224 (1984) 697-701
    • (1984) Biochem. J , vol.224 , pp. 697-701
    • Gutteridge, J.M.C.1
  • 8
    • 0027050315 scopus 로고
    • Cellular regulation of the iron responsive element binding protein-Disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding
    • Haile D.J., Rouault T.A., Harford J.B., Kennedy M.C., Blondin G.A., Beinert H., and Klausner R.D. Cellular regulation of the iron responsive element binding protein-Disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding. Proc. Natl. Acad. Sci. USA 89 (1992) 11735-11739
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11735-11739
    • Haile, D.J.1    Rouault, T.A.2    Harford, J.B.3    Kennedy, M.C.4    Blondin, G.A.5    Beinert, H.6    Klausner, R.D.7
  • 10
    • 0017229026 scopus 로고
    • Oxido-reductive titrations of cytochrome c oxidase followed by EPR spectroscopy
    • Hartzell C.R., and Beinert H. Oxido-reductive titrations of cytochrome c oxidase followed by EPR spectroscopy. Biochim. Biophys. Acta 423 (1976) 323-338
    • (1976) Biochim. Biophys. Acta , vol.423 , pp. 323-338
    • Hartzell, C.R.1    Beinert, H.2
  • 11
    • 0642342084 scopus 로고    scopus 로고
    • Evolutionary biology: Essence of mitochondria
    • Henze K., and Martin W. Evolutionary biology: Essence of mitochondria. Nature 426 (2003) 127-128
    • (2003) Nature , vol.426 , pp. 127-128
    • Henze, K.1    Martin, W.2
  • 12
    • 34548445911 scopus 로고    scopus 로고
    • Electron paramagnetic resonance and Mössbauer spectroscopy of intact mitochondria from respiring Saccharomyces cerevisiae
    • Hudder N., Morales J.G., Stubna A., Münck E., Hendrich M.P., and Lindahl P.A. Electron paramagnetic resonance and Mössbauer spectroscopy of intact mitochondria from respiring Saccharomyces cerevisiae. J. Biol. Inorg. Chem. 12 (2007) 1029-1053
    • (2007) J. Biol. Inorg. Chem. , vol.12 , pp. 1029-1053
    • Hudder, N.1    Morales, J.G.2    Stubna, A.3    Münck, E.4    Hendrich, M.P.5    Lindahl, P.A.6
  • 13
    • 0017099205 scopus 로고
    • Cytochrome bc1 complex of yeast mitochondria-Isolation and partial characterization of cytochrome bc1 complex and cytochrome b
    • Katan M.B., Pool L., and Groot G.S.P. Cytochrome bc1 complex of yeast mitochondria-Isolation and partial characterization of cytochrome bc1 complex and cytochrome b. Eur. J. Biochem. 65 (1976) 95-105
    • (1976) Eur. J. Biochem. , vol.65 , pp. 95-105
    • Katan, M.B.1    Pool, L.2    Groot, G.S.P.3
  • 14
    • 0034255836 scopus 로고    scopus 로고
    • Maturation of cellular Fe-S proteins: an essential function of mitochondria
    • Lill R., and Kispal G. Maturation of cellular Fe-S proteins: an essential function of mitochondria. Trends Biochem. Sci. 25 (2000) 352-356
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 352-356
    • Lill, R.1    Kispal, G.2
  • 16
    • 0041893905 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur proteins in eukaryotes: A novel task of mitochondria that is inherited from bacteria. Biochim. Biophys
    • Mühlenhoff U., and Lill R. Biogenesis of iron-sulfur proteins in eukaryotes: A novel task of mitochondria that is inherited from bacteria. Biochim. Biophys. Acta Bioenergetics 1459 (2000) 370-382
    • (2000) Acta Bioenergetics , vol.1459 , pp. 370-382
    • Mühlenhoff, U.1    Lill, R.2
  • 17
    • 2242453224 scopus 로고    scopus 로고
    • Characterization of iron-sulfur protein assembly in isolated mitochondria-A requirement for ATP, NADH, and reduced iron
    • Mühlenhoff U., Richhardt N., Gerber J., and Lill R. Characterization of iron-sulfur protein assembly in isolated mitochondria-A requirement for ATP, NADH, and reduced iron. J. Biol. Chem. 277 (2002) 29810-29816
    • (2002) J. Biol. Chem. , vol.277 , pp. 29810-29816
    • Mühlenhoff, U.1    Richhardt, N.2    Gerber, J.3    Lill, R.4
  • 18
    • 0018064716 scopus 로고
    • Mössbauer spectroscopy of proteins: Electron carriers
    • Münck E. Mössbauer spectroscopy of proteins: Electron carriers. Methods Enzymol. 54 (1978) 346-379
    • (1978) Methods Enzymol. , vol.54 , pp. 346-379
    • Münck, E.1
  • 19
    • 0027330259 scopus 로고
    • Combining Mössbauer spectroscopy with integer spin electron paramagnetic resonance
    • Münck E., Surerus K.K., and Hendrich M.P. Combining Mössbauer spectroscopy with integer spin electron paramagnetic resonance. Methods Enzymol. 227 (1993) 463-479
    • (1993) Methods Enzymol. , vol.227 , pp. 463-479
    • Münck, E.1    Surerus, K.K.2    Hendrich, M.P.3
  • 20
    • 0037132531 scopus 로고    scopus 로고
    • The PLP-dependent biotin synthase from Escherichia coli: Mechanistic studies
    • Ollagnier-de-Choudens S., Mulliez E., and Fontecave M. The PLP-dependent biotin synthase from Escherichia coli: Mechanistic studies. FEBS Let. 532 (2002) 465-468
    • (2002) FEBS Let. , vol.532 , pp. 465-468
    • Ollagnier-de-Choudens, S.1    Mulliez, E.2    Fontecave, M.3
  • 21
    • 0345120596 scopus 로고    scopus 로고
    • The lipoate synthase from Escherichia coli is an iron-sulfur protein
    • Ollagnier-de-Choudens S., and Fontecave M. The lipoate synthase from Escherichia coli is an iron-sulfur protein. FEBS Let. 453 (1999) 25-28
    • (1999) FEBS Let. , vol.453 , pp. 25-28
    • Ollagnier-de-Choudens, S.1    Fontecave, M.2
  • 22
    • 0017109543 scopus 로고
    • NADH-ubiquinone oxidoreductase
    • Ragan C.I. NADH-ubiquinone oxidoreductase. Biochim. Biophys. Acta 456 (1976) 249-290
    • (1976) Biochim. Biophys. Acta , vol.456 , pp. 249-290
    • Ragan, C.I.1
  • 23
    • 34547602992 scopus 로고    scopus 로고
    • Assessment of chelatable mitochondrial iron by using mitochondrion-selective fluorescent iron indicators with different iron-binding affinities
    • Rauen U., Springer A., Weisheit D., Petrat F., Korth H.-G., deGroot H., and Sustmann R. Assessment of chelatable mitochondrial iron by using mitochondrion-selective fluorescent iron indicators with different iron-binding affinities. Chem. Biochem. 8 (2007) 341-352
    • (2007) Chem. Biochem. , vol.8 , pp. 341-352
    • Rauen, U.1    Springer, A.2    Weisheit, D.3    Petrat, F.4    Korth, H.-G.5    deGroot, H.6    Sustmann, R.7
  • 24
    • 0002345887 scopus 로고
    • Studies on mitochondria and submitochondrial particles by paramagnetic resonance (EPR) spectroscopy
    • Sands R.H., and Beinert H. Studies on mitochondria and submitochondrial particles by paramagnetic resonance (EPR) spectroscopy. Biochem. Biophys. Res. Comm. 3 (1960) 47-52
    • (1960) Biochem. Biophys. Res. Comm. , vol.3 , pp. 47-52
    • Sands, R.H.1    Beinert, H.2
  • 25
    • 0018787277 scopus 로고
    • Purification of a reconstitutively active iron-sulfur protein (oxidation factor) from succinate cytochrome c reductase complex of bovine heart mitochondria
    • Trumpower B.L., and Edwards C.A. Purification of a reconstitutively active iron-sulfur protein (oxidation factor) from succinate cytochrome c reductase complex of bovine heart mitochondria. J. Biol. Chem. 254 (1979) 8697-8706
    • (1979) J. Biol. Chem. , vol.254 , pp. 8697-8706
    • Trumpower, B.L.1    Edwards, C.A.2
  • 26
    • 0022555846 scopus 로고
    • Genetics of mitochondrial biogenesis
    • Tzagoloff A., and Myers A.M. Genetics of mitochondrial biogenesis. Ann. Rev. Biochem. 55 (1986) 249-285
    • (1986) Ann. Rev. Biochem. , vol.55 , pp. 249-285
    • Tzagoloff, A.1    Myers, A.M.2
  • 27
    • 33846390427 scopus 로고    scopus 로고
    • Building the power house: Recent advances in mitochondrial studies through proteomics and systems biology
    • Vo T.D., and Palsson B.O. Building the power house: Recent advances in mitochondrial studies through proteomics and systems biology. Am. J. Physiol. Cell Physiol. 292 (2007) C164-C177
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Vo, T.D.1    Palsson, B.O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.