Mass spectrometric characterization of mitochondrial electron transport complexes: Subunits of the rat heart ubiquinol-cytochrome c reductase

Journal of Mass Spectrometry

Volumn 38, Issue 5, 2003, Pages 531-539

  Sun, Gang ^a   Kinter, Michael T ^b   Anderson, Vernon E ^a  

^a CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b LERNER RESEARCH INSTITUTE   (United States)

Author keywords

BN PAGE; Electron transport complex; In gel digestion; Matrix assisted laser desorption ionization mass spectrometry; Membrane proteins; Native electroelution; Tricine sodium dodecyl sulfate polyacrylamide gel electrophoresis; Ubiquinol cytochrome c reductase

Indexed keywords

COMPLEXATION; ELECTROPHORESIS; GELS; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; PATHOLOGY; POLYPEPTIDES;

ELECTRON TRANSPORT COMPLEXES;

ELECTRON TRANSITIONS;

CHYMOTRYPSIN; CYTOCHROME C; DODECYL SULFATE SODIUM; IRON SULFUR PROTEIN; MEMBRANE ENZYME; POLYPEPTIDE; PROTEIN SUBUNIT; TRYPSIN; UBIQUINOL CYTOCHROME C REDUCTASE;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DISORDERS OF MITOCHONDRIAL FUNCTIONS; ELUTION; ENZYME ISOLATION; HEART MITOCHONDRION; LIQUID CHROMATOGRAPHY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MITOCHONDRIAL ENERGY TRANSFER; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PATHOGENESIS; PEPTIDE ANALYSIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN MODIFICATION; RAT; TANDEM MASS SPECTROMETRY;

AMINO ACID SEQUENCE; ANIMALS; ELECTRON TRANSPORT; ELECTRON TRANSPORT COMPLEX III; ELECTROPHORESIS, POLYACRYLAMIDE GEL; MITOCHONDRIA, HEART; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; RATS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; TRYPSIN;

EID: 0038617425     PISSN: 10765174     EISSN: None     Source Type: Journal    
DOI: 10.1002/jms.467     Document Type: Article

References (30)

1. Schagger H, von Jagow G. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 1991; 199: 223.
2. Schagger H. Blue-native gels to isolate protein complexes from mitochondria. Methods Cell Biol. 2001; 65: 231.
3. Poetsch A, Neff D, Seelert H, Schagger H, Dencher NA. Dye removal, catalytic activity and 2d crystallization of chloroplast H(+)-ATP synthase purified by blue native electrophoresis. Biochim. Biophys. Acta 2000; 1466: 339.
4. Grandier-Vazeille X, Guerin M. Separation by blue native and colorless native polyacrylamide gel electrophoresis of the oxidative phosphorylation complexes of yeast mitochondria solubilized by different detergents: specific staining of the different complexes. Anal. Biochem. 1996; 242: 248.
5. Dawson TL, Gores GJ, Nieminen AL, Herman B, Lemasters JJ. Mitochondria as a source of reactive oxygen species during reductive stress in rat hepatocytes. Am. J. Physiol. 1993; 264: C961.
6. Lesnefsky EJ, Gudz TI, Migita CT, Ikeda-Saito M, Hassan MO, Turkaly PJ, Hoppel CL. Ischemic injury to mitochondrial electron transport in the aging heart: damage to the iron-sulfur protein subunit of electron transport complex III. Arch. Biochem. Biophys. 2001; 385: 117.
7. Lesnefsky EJ, Gudz TI, Moghaddas S, Migita CT, Ikeda-Saito M, Turkaly PJ, Hoppel CL. Aging decreases electron transport complex III activity in heart interfibrillar mitochondria by alteration of the cytochrome c binding site. J. Mol. Cell. Cardiol. 2001; 33: 37.
8. Johnson WT, Thomas AC. Copper deprivation potentiates oxidative stress in hl-60 cell mitochondria. Proc. Soc. Exp. Biol. Med. 1999; 221: 147.
9. Chen J, Robinson NC, Schenker S, Frosto TA, Henderson GI. Formation of 4-hydroxynonenal adducts with cytochrome c oxidase in rats following short-term ethanol intake. Hepatology 1999; 29: 1792.
10. Palmer JW, Tandler B, Hoppel CL. Biochemical properties of subsarcolemmal and interfibrillar mitochondria isolated from rat cardiac muscle. J. Biol. Chem. 1977; 252: 8731.
11. Lesnefsky EJ, Tandler B, Ye J, Slabe TJ, Turkaly J, Hoppel CL. Myocardial ischemia decreases oxidative phosphorylation through cytochrome oxidase in subsarcolemmal mitochondria. Am. J. Physiol. 1997; 273: H1544.
12. Schagger H, Cramer WA, von Jagow G. Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 1994; 217: 220.
13. Ehring H, Stromberg S, Tjernberg A, Noren B. Matrix-assisted laser desorption/ionization mass spectrometry of proteins extracted directly from sodium dodecyl sulphate-polyacrylamide gels. Rapid Commun. Mass Spectrom. 1997; 11: 1867.
14. Vestling MM, Fenselau C. Polyvinylidene difluoride (PVDF): an interface for gel electrophoresis and matrix-assisted laser desorption/ionization mass spectrometry. Biochem. Soc. Trans. 1994; 22: 547.
15. Goeddel DV, Kleid DG, Bolivar F, Heyneker HL, Yansura DG, Crea R, Hirose T, Kraszewski A, Itakura K, Riggs AD. Expression in E. coli of chemically synthesized genes for human insulin. Proc. Nat. Acad. Sci. USA 1979; 76: 106.
16. Jensen PK, Pasa-Tolic L, Anderson GA, Horner JA, Lipton MS, Bruce JE, Smith RD. Probing proteomes using capillary isoelectric focusing-electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 1999; 71: 2076.
17. Pearson WR, Lipman DJ. Improved tools for biological sequence comparison. Proc. Nat. Acad. Sci. USA 1988; 85: 2444.
18. Ghaim JB, Tsatsos PH, Katsonouri A, Mitchell DM, Salcedo-Hernandez R, Gennis RB. Matrix-assisted laser desorption ionization mass spectrometry of membrane proteins: demonstration of a simple method to determine subunit molecular weights of hydrophobic subunits. Biochim. Biophys. Acta 1997; 1330: 113.
19. Brookes PS, Pinner A, Ramachandran A, Coward L, Barnes S, Kim H, Darley-Usmar VM. High throughput two-dimensional blue-native electrophoresis: a tool for functional proteomics of mitochondria and signaling complexes. Proteomics 2002; 2: 969.
20. Sone N, Takagi T. Monomer-dimer structure of cytochrome-c oxidase and cytochrome bc1 complex from the thermophilic bacterium ps3. Biochim. Biophys. Acta 1990; 1020: 207.
21. Xia D, Yu CA, Kim H, Xia JZ, Kachurin AM, Zhang L, Yu L, Deisenhofer J. Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria. Science 1997; 277: 60.
22. Benson D, Boguski M, Lipman DJ, Ostell J. Genbank. Nucleic Acids Res. 1994; 22: 3441.
23. Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ. Basic local alignment search tool. J. Mol. Biol. 1990; 215: 403.
24. Boguski MS, Lowe TM, Tolstoshev CM. DbEST - database for 'expressed sequence tags.' Nature Genet. 1993; 4: 332.
25. Musatov A, Robinson NC. Subunit analysis of bovine cytochrome bc1 by reverse-phase HPLC and determination of the subunit molecular masses by electrospray ionization mass spectrometry. Biochemistry 1994; 33: 10561.
26. Nishikimi M, Hosokawa Y, Toda H, Suzuki H, Ozawa T. Cloning and sequence analysis of a cDNA encoding the Rieske iron-sulfur protein of rat mitochondrial cytochrome bc1 complex. Biochem. Biophys. Res. Commun. 1989; 159: 19.
27. Moos M Jr, Nguyen Nga Y, Liu TY. Reproducible high yield sequencing of proteins electrophoretically separated and transferred to an inert support. J. Biol. Chem. 1988; 263: 6005.
28. Gygi SP, Rist B, Gerber SA, Turecek F, Gelb MH, Aebersold R. Quantitative analysis of complex protein mixtures using isotopecoded affinity tags. Nature Biotechnol. 1999; 17: 994.
29. Hosokawa Y, Suzuki H, Toda H, Nishikimi M, Ozawa T. The primary structure of the precursor to core protein II, a putative member of mitochondrial processing protease family, of rat mitochondrial cytochrome bc1 complex deduced from cDNA sequence analysis. Biochem. Int. 1990; 20: 731.
30. Goertz G, Feldmann H. Nucleotide sequence of the cytochrome b gene and adjacent regions from rat liver mitochondrial DNA. Curr. Genet. 1982; 5: 221.