Quinone electrophiles selectively adduct "electrophile binding motifs" within cytochrome c

Biochemistry

Volumn 46, Issue 39, 2007, Pages 11090-11100

  Fisher, Ashley A ^a   Labenski, Matthew T ^a   Malladi, Srinivas ^b   Gokhale, Vijay ^a   Bowen, Martina E ^a   Milleron, Rania S ^b   Bratton, Shawn B ^b   Monks, Terrence J ^a   Lau, Serrine S ^a  

^a UNIVERSITY OF ARIZONA   (United States)

^b UNIVERSITY OF TEXAS AT AUSTIN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSOME COMPLEXES; ELECTROPHILE BINDING MOTIFS; NUCLEOPHILIC SITES; POST TRANSLATIONAL MODIFICATIONS; QUINONE ELECTROPHILES;

AMINO ACIDS; CARCINOGENS; GENE EXPRESSION; ION SOURCES; METABOLISM; MOLECULAR MODELING; NUCLEOPHILES; OXIDATION; TOXICITY;

PROTEINS;

1,4 BENZOQUINONE; 2 (N ACETYLCYSTEIN S YL)BENZOQUINONE; ACETYLCYSTEINE; AMINO ACID; APOPTOSOME; APOPTOTIC PROTEASE ACTIVATING FACTOR 1; CASPASE 3; CYTOCHROME C; GLUTAMIC ACID; HYDROQUINONE; LYSINE; PROTEIN; SOLVENT; SULFIDE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; HUMAN CELL; MASS SPECTROMETRY; MOLECULAR MODEL; NUCLEOTIDE SEQUENCE; OLIGOMERIZATION; OXIDATION; PKA; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; SEQUENCE ANALYSIS;

ACETYLCYSTEINE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; APOPTOSOMES; BENZOQUINONES; CASPASE 3; CASPASE 9; CELL LINE, TUMOR; CHROMATOGRAPHY, LIQUID; CIRCULAR DICHROISM; CYTOCHROMES C; HORSES; HUMANS; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; TANDEM MASS SPECTROMETRY;

RATTUS;

EID: 34848871967     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700613w     Document Type: Article

References (30)

1. Cohen, S. D., Pumford, N. R., Khairallah, E. A., Boekelheide, K., Pohl, L. R., Amouzadeh, H. R., and Hinson, J. A. (1997) Selective protein covalent binding and target organ toxicity, Toxicol. Appl. Pharmacol. 143, 1-12.
2. Zhou, S., Chan, E., Duan, W., Huang, M., and Chen, Y. Z. (2005) Drug bioactivation, covalent binding to target proteins and toxicity relevance, Drug Metab. Rev. 37, 41-213.
3. Person, M. D., Mason, D. E., Liebler, D. C., Monks, T. J., and Lau, S. S. (2005) Alkylation of cytochrome c by (glutathion-S-yl)-1,4-benzoquinone and iodoacetamide demonstrates compound-dependent site specificity, Chem. Res. Toxicol. 18, 41-50.
4. Person, M. D., Monks, T. J., and Lau, S. S. (2003) An integrated approach to identifying chemically induced posttranslational modifications using comparative MALDI-MS and targeted HPLC-ESI-MS/MS, Chem. Res. Toxicol. 16, 598-608.
5. Guengerich, F. P., and Liebler, D. C. (1985) Enzymatic activation of chemicals to toxic metabolites, Crit. Rev. Toxicol. 14, 259-307.
6. Ross, D. (2000) The role of metabolism and specific metabolites in benzene-induced toxicity: Evidence and issues, J. Toxicol. Environ. Health, Part A 61, 357-372.
7. Pagano, G. (2002) Redox-modulated xenobiotic action and ROS formation: A mirror or a window? Hum. Exp. Toxicol. 21, 77-81.
8. Bolton, J. L., Trush, M. A., Penning, T. M., Dryhurst, G., and Monks, T. J. (2000) Role of quinones in toxicology, Chem. Res. Toxicol. 13, 135-160.
9. Verrax, J., Delvaux, M., Beghein, N., Taper, H., Gallez, B., and Buc Calderon, P. (2005) Enhancement of quinone redox cycling by ascorbate induces a caspase-3 independent cell death in human leukaemia cells. An in vitro comparative study, Free Radical Res. 39, 649-657.
10. Ruiz-Ramos, R., Cebrian, M. E., and Garrido, E. (2005) Benzoquinone activates the ERK/MAPK signaling pathway via ROS production in HL-60 cells, Toxicology 209, 279-287.
11. Lindsey, R. H., Jr., Bender, R. P., and Osheroff, N. (2005) Effects of benzene metabolites on DNA cleavage mediated by human topoisomerase IIα: 1,4-Hydroquinone is a topoisomerase II poison, Chem. Res. Toxicol. 18, 761-770.
12. Lau, S. S., Hill, B. A., Highet, R. J., and Monks, T. J. (1988) Sequential oxidation and glutathione addition to 1,4-benzoquinone: Correlation of toxicity with increased glutathione substitution, Mol. Pharmacol. 34, 829-836.
13. Peters, M. M., Jones, T. W., Monks, T. J., and Lau, S. S. (1997) Cytotoxicity and cell-proliferation induced by the nephrocarcinogen hydroquinone and its nephrotoxic metabolite 2,3,5-(trisglutathion-S-yl)hydroquinone, Carcinogenesis 18, 2393-2401.
14. Kleiner, H. E., Jones, T. W., Monks, T. J., and Lau, S. S. (1998) Immunochemical analysis of quinol-thioether-derived covalent protein adducts in rodent species sensitive and resistant to quinolthioether-mediated nephrotoxicity, Chem. Res. Toxicol. 11, 1291-1300.
15. Yoon, H. S., Monks, T. J., Walker, C. L., and Lau, S. S. (2001) Transformation of kidney epithelial cells by a quinol thioether via inactivation of the tuberous sclerosis-2 tumor suppressor gene, Mol. Carcinog. 31, 37-45.
16. Bratton, S. B., Walker, G., Srinivasula, S. M., Sun, X. M., Butterworth, M., Alnemri, E. S., and Cohen, G. M. (2001) Recruitment, activation and retention of caspases-9 and -3 by Apaf-1 apoptosome and associated XIAP complexes, EMBO J. 20, 998-1009.
17. Bratton, S. B., Walker, G., Roberts, D. L., Cain, K., and Cohen, G. M. (2001) Caspase-3 cleaves Apaf-1 into an approximately 30 kDa fragment that associates with an inappropriately oligomerized and biologically inactive approximately 1.4 MDa apoptosome complex, Cell Death Differ. 8, 425-433.
18. Craig, R., and Beavis, R. C. (2003) A method for reducing the time required to match protein sequences with tandem mass spectra, Rapid Commun. Mass Spectrom. 17, 2310-2316.
19. Craig, R., Cortens, J. P., and Beavis, R. C. (2004) Open source system for analyzing, validating, and storing protein identification data, J. Proteome Res. 3, 1234-1242.
20. Hansen, B. T., Davey, S. W., Ham, A. J., and Liebler, D. C. (2005) P-Mod: An algorithm and software to map modifications to peptide sequences using tandem MS data, J. Proteome Res. 4, 358-368.
21. Standing, K. G. (2003) Peptide and protein de novo sequencing by mass spectrometry, Curr. Opin. Struct. Biol. 13, 595-601.
22. Bushneil, G. W., Louie, G. V., and Brayer, G. D. (1990) High-resolution three-dimensional structure of horse heart cytochrome c, J. Mol. Biol. 214, 585-595.
23. Insight 11 (2000) Accelrys Inc., San Diego.
24. Discover_3 ESFF (extensible systematic force field). Molecular mechanics force fields, Insight 11, 2000.3L (2000) Accelrys, Inc., San Diego.
25. Jorgensen, W. L., Chandrasekhar, J., Madura, J. D., Impey, R. W., and Klein, M. L. (1983) Comparison of simple potential functions for simulating liquid water, J. Chem. Phys. 79, 926-935.
26. Cain, K., Bratton, S. B., Langlais, C., Walker, G., Brown, D. G., Sun, X. M., and Cohen, G. M. (2000) Apaf-1 oligomerizes into biologically active approximately 700-kDa and inactive approximately 1.4-MDa apoptosome complexes, J. Biol. Chem. 275, 6067-6070.
27. Yu, T., Wang, X., Purring-Koch, C., Wei, Y., and McLendon, G. L. (2001) A mutational epitope for cytochrome C binding to the apoptosis protease activation factor-1, J. Biol. Chem. 276, 13034-13038.
28. Shi, Y. (2002) Apoptosome: The cellular engine for the activation of caspase-9, Structure 10, 285-288.
29. Chandra, D., Bratton, S. B., Person, M. D., Tian, Y., Martin, A. G., Ayres, M., Fearnhead, H. O., Gandhi, V., and Tang, D. G. (2006) Intracellular nucleotides act as critical prosurvival factors by binding to cytochrome c and inhibiting apoptosome, Cell 125, 1333-1346.
30. Samali, A., O'Mahoney, M., Reeve, J., Logue, S., Szegezdi, E., McMahon, J., and Fearnhead, H. O. (2007) Identification of an inhibitor of caspase activation from heart extracts: ATP blocks apoptosome formation, Apoptosis 12, 465-474.