Architecture of succinate dehydrogenase and reactive oxygen species generation

Science

Volumn 299, Issue 5607, 2003, Pages 700-704

  Yankovskaya, Victoria ^a   Horsefield, Rob ^b   Törnroth, Susanna ^c   Luna Chavez, César ^a,d,g   Miyoshi, Hideto ^e   Léger, Christophe ^f,h   Byrne, Bernadette ^b   Cecchini, Gary ^a,d   Iwata, So ^b,c  

^a VETERANS AFFAIRS MEDICAL CENTER   (United States)

^b IMPERIAL COLLEGE LONDON   (United Kingdom)

^c UPPSALA UNIVERSITY   (Sweden)

^d UNIVERSITY OF CALIFORNIA   (United States)

^e KYOTO UNIVERSITY   (Japan)

^f UNIVERSITY OF OXFORD   (United Kingdom)

^g UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^h BIP07 CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

DEHYDROGENATION; ESCHERICHIA COLI; OXYGEN;

ELECTRON TRANSPORT PATHWAY;

ENZYMES;

BACTERIAL ENZYME; FLAVINE ADENINE NUCLEOTIDE; FUMARATE REDUCTASE; REACTIVE OXYGEN METABOLITE; SUCCINATE DEHYDROGENASE; SUCCINIC ACID; UBIQUINONE;

ELECTRON; ENZYME;

AEROBIC METABOLISM; ARTICLE; ELECTRON TRANSPORT; ENZYME STRUCTURE; ESCHERICHIA COLI; GENE MUTATION; MITOCHONDRIAL RESPIRATION; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL;

AEROBIOSIS; ANAEROBIOSIS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DINITROPHENOLS; ELECTRON TRANSPORT; ELECTRON TRANSPORT COMPLEX II; ESCHERICHIA COLI; FLAVIN-ADENINE DINUCLEOTIDE; HEME; MODELS, MOLECULAR; MULTIENZYME COMPLEXES; MUTATION; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; REACTIVE OXYGEN SPECIES; SUCCINATE DEHYDROGENASE; SUCCINIC ACID; SUPEROXIDES; UBIQUINONE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0348150715     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1079605     Document Type: Article

References (33)

1. For a review, see G. Cecchini, I. Schröder, R. P. Gunsalus, E. Maklashina, Biochim. Biophys. Acta 1553, 140 (2002).
2. For a review, see P. Rustin, A. Rötig, Biochim. Biophys. Acta 1553, 117 (2002).
3. T. Bourgeron et al., Nature Genet. 11, 144 (1995).
4. B. E. Baysal et al., Science 287, 848 (2000).
5. S. Niemann, U. Müller, Nature Genet. 26, 268 (2000).
6. N. Ishii et al., Nature 394, 694 (1998).
7. N. Senoo-Matsuda et al., J. Biol. Chem. 276, 41553 (2001).
8. A. Kröger, V. Geisler, E. Lemma, F. Theis, R. Lenger, Arch. Microbiol. 158, 311 (1992).
9. For a review, see L. Hederstedt, Science 284, 1941 (1999).
10. J. R. Guest, J. Gen. Microbiol. 122, 171 (1981).
11. E. Maklashina, D. A. Berthold, G. Cecchini, J. Bacteriol. 180, 5989 (1998).
12. T. M. Iverson, C. Luna-Chavez, G. Cecchini, D. C. Rees, Science 284, 1961 (1999).
13. C. R. D. Lancaster, A. Kröger, M. Auer, H. Michel, Nature 402, 377 (1999).
14. K. Kita, H. Hirawake, H. Miyadera, H. Amino, S. Takeo, Biochim. Biophys. Acta 1553, 123 (2002).
15. J. J. Van Hellmond, A. G. M. Tielens, Biochem. J. 304, 321 (1994).
16. Materials and methods are available as supporting material on Science Online.
17. T. A. Jones, J. Y. Zou, S. W. Cowan, M. Kjeldgaard, Acta Crystallogr. A47, 110 (1991).
18. B. A. C. Ackrell, B. Cochran, G. Cecchini, Arch. Biochem. Biophys. 268, 26 (1989).
19. C. Hägerhäll, Biochim. Biophys. Acta 1320, 107 (1997).
20. M. T. Werth et al., FEBS Lett. 299, 1 (1992).
21. W. R. Hagen et al., J. Biol. Inorg. Chem. 5, 527 (2000).
22. C. C. Page, C. C. Moser, X. Chen, P. L. Dutton, Nature 402, 47 (1999).
23. E. Maklashina, R. A. Rothery, J. H. Weiner, G. Cecchini. J. Biol. Chem. 276, 18968 (2001).
24. V. Yankovskaya et al., J. Biol. Chem. 271, 21020 (1996).
25. N. Fisher, P. R. Rich, J. Mol. Biol. 296, 1153 (2000).
26. M. Jormakka, S. Törnroth, B. Byrne, S. Iwata, Science 295, 1863 (2002).
27. D. Astuti et al., Am. J. Hum. Genet. 69, 49 (2001).
28. B. E. Baysal, J. Med. Genet. 39, 617 (2002).
29. K. R. Messner, J. A. Imlay, J. Biol. Chem. 277, 42563 (2002).
30. L. Yu, J.-X. Xu, P. E. Haley, C.-A. Yu, J. Biol. Chem. 262, 1137 (1987).
31. C. Hägerhäll et al., J. Biol. Chem. 274, 26157 (1999).
32. F. J. Ruzicka, H. Beinert, K. L. Schepler, W. R. Dunham, R. H. Sands, Proc. Natl. Acad. Sci. U.S.A. 72, 2886 (1975).
33. Supported by Biotechnology and Biological Science Research Council of the UK, Structural Biology Network of Sweden, Syngenta, and the Department of Veterans Affairs and NIH grant GM61606, We thank E. Mitchell and A. Thompson at ESRF, Grenoble, and T. Tomizaki and C. Schulze-Briese at SLS for technical assistance. We also thank J. Abramson and T. Iverson for critically reading the manuscript. The coordinates for the native SQR and the DNP-17 complex are deposited with PDB (entries 1NEK and 1NEN, respectively).