Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin

Biochemistry

Volumn 44, Issue 31, 2005, Pages 10583-10592

  Parsonage, Derek ^a   Youngblood, Derek S ^b   Sarma, Ganapathy N ^b   Wood, Zachary A ^b   Karplus, P Andrew ^b   Poole, Leslie B ^a  

^a WAKE FOREST SCHOOL OF MEDICINE   (United States)

^b OREGON STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOCHEMISTRY; CONCENTRATION (PROCESS); MUTAGENESIS; OLIGOMERS; PHYSIOLOGY; PROTEINS; REDOX REACTIONS;

OXIDANT PROTECTION; PEROXIREDOXINS; SIGNAL TRANSDUCTION;

ENZYME INHIBITION;

AHPC PROTEIN; BACTERIAL ENZYME; CYSTEINE; HYDROGEN PEROXIDE; MUTANT PROTEIN; OLIGOMER; PEROXIDASE; PEROXIREDOXIN; THREONINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CRYSTALLOGRAPHY; ENZYME ACTIVITY; ENZYME ANALYSIS; MEASUREMENT; MOLECULAR DYNAMICS; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; SALMONELLA TYPHIMURIUM; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS; ULTRACENTRIFUGATION;

BACTERIAL PROTEINS; BINDING SITES; CATALYSIS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ENZYME ACTIVATION; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PEROXIDASES; PEROXIDES; SALMONELLA TYPHIMURIUM; THREONINE;

SALMONELLA TYPHIMURIUM;

EID: 23244466487     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050448i     Document Type: Article

References (26)

1. Poole, L. B., Godzik, A., Nayeem, A., and Schmitt, J. D. (2000) AhpF can be dissected into two functional units: Tandem repeats of two thioredoxin-like folds in the N-terminus mediate electron transfer from the thioredoxin reductase-like C-terminus to AhpC, Biochemistry 39, 6602-6615.
2. Hofmann, B., Hecht, H.-J., and Flohé, L. (2002) Peroxiredoxins, Biol. Chem. 383, 347-364.
3. Wood, Z. A., Poole, L. B., and Karplus, P. A. (2003) Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling, Science 300, 650-653.
4. Wood, Z. A., Schroder, E., Harris, J. R., and Poole, L. B. (2003) Structure, mechanism and regulation of peroxiredoxins, Trends Biochem. Sci. 28, 32-40.
5. Poole, L. B., Reynolds, C. M., Wood, Z. A., Karplus, P. A., Ellis, H. R., and Li Calzi, M. (2000) AhpF and other NADH: peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase, Eur. J. Biochem. 267, 6126-6133.
6. Wood, Z. A., Poole, L. B., Hantgan, R. R., and Karplus, P. A. (2002) Dimers to doughnuts: Redox-sensitive oligomerization of 2-cysteine peroxiredoxins, Biochemistry 41, 5493-5504.
7. Georgiou, G., and Masip, L. (2003) An overoxidation journey with a return ticket, Science 300, 592-594.
8. Poole, L. B., and Ellis, H. R. (1996) Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins, Biochemistry 35, 56-64.
9. Reynolds, C. M., and Poole, L. B. (2000) Attachment of the N-terminal domain of Salmonella typhimurium AhpF to Escherichia coli thioredoxin reductase confers AhpC reductase activity but does not affect thioredoxin reductase activity, Biochemistry 39, 8859-8869.
10. Laue, T. M., Shah, B. D., Ridgeway, T. M., and Pelletier, S. L. (1992) Computer-aided interpretation of analytical sedimentation data for proteins, in Analytical ultracentrifugation in biochemistry and polymer science (Harding, S. E., Rowe, A. J., and Horton, J. C., Eds.) pp 90-125, The Royal Society of Chemistry, Cambridge, U.K.
11. Van Holde, K. E. (1971) Physical Biochemistry, pp 110-136, Prentice-Hall, Inc., Englewood Cliffs, NJ.
12. Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination, Acta Crystallogr. D54 (Part 5), 905-921.
13. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47 (Part 2), 110-119.
14. Laskowski, R. A., Moss, D. S., and Thornton, J. M. (1993) Mainchain bond lengths and bond angles in protein structures, J. Mol. Biol. 231, 1049-1067.
15. 2-forming NADH oxidase is an alkyl hydroperoxide reductase protein, Free Radical Biol. Med. 28, 108-120.
16. Li Calzi, M., and Poole, L. B. (1997) Requirement for the two AhpF cystine disulfide centers in catalysis of peroxide reduction by alkyl hydroperoxide reductase, Biochemistry 36, 13357-13364.
17. Poole, L. B. (1999) Flavin-linked redox components required for AhpC reduction in alkyl hydroperoxide reductase systems, in Flavins and Flavoproteins 1999 (Ghisla, S., Kroneck, P., Macheroux, P., and Sund, H., Eds.) pp 691-694, Agency for Scientific Publications, Berlin.
18. Holmgren, A. (1972) Tryptophan fluorescence study of conformational transitions of the oxidized and reduced form of thioredoxin, J. Biol. Chem. 247, 1992-1998.
19. Baker, L. M., and Poole, L. B. (2003) Catalytic mechanism of thiol peroxidase from Escherichia coli. Sulfenic acid formation and overoxidation of essential CYS61, J. Biol. Chem. 278, 9203-9211.
20. Akerman, S. E., and Müller, S. (2005) Peroxiredoxin-linked detoxification of hydroperoxides in Toxoplasma gondii, J. Biol. Chem. 280, 564-570.
21. Baker, L. M., Raudonikiene, A., Hoffman, P. S., and Poole, L. B. (2001) Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: Genetic and kinetic characterization, J. Bacteriol. 183, 1961-1973.
22. Chang, T. S., Jeong, W., Choi, S. Y., Yu, S., Kang, S. W., and Rhee, S. G. (2002) Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation, J. Biol. Chem. 277, 25370-25376.
23. Breinig, S., Kervinen, J., Stith, L., Wasson, A. S., Fairman, R., Wlodawer, A., Zdanov, A., and Jaffe, E. K. (2003) Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase, Nat. Struct. Biol. 10, 757-763.
24. Copley, S. D., Novak, W. R., and Babbitt, P. C. (2004) Divergence of function in the thioredoxin fold suprafamily: Evidence for evolution of peroxiredoxins from a thioredoxin-like ancestor, Biochemistry 43, 13981-13995.
25. Sarma, G. N., Nickel, C., Rahlfs, S., Fischer, M., Becker, K., and Karplus, P. A. (2005) Crystal structure of a novel Plasmodium falciparum 1-Cys peroxiredoxin, J. Mol. Biol. 346, 1021-1034.
26. Diederichs, K., and Karplus, P. A. (1997) Improved R-factors for diffraction data analysis in macromolecular crystallography, Nat. Struct. Biol. 4, 269-275.