The iron-sulfur cluster of pyruvate formate-lyase activating enzyme in whole cells: Cluster interconversion and a valence-localized [4Fe-4S] 2+ state

Biochemistry

Volumn 48, Issue 39, 2009, Pages 9234-9241

  Yang, Jian ^b   Naik, Sunil G ^c   Ortillo, Danilo O ^c   García Serres, Ricardo ^c,d   Li, Meng ^b   Broderick, William E ^a   Boi, Hanh Huynh ^c   Broderick, Joan B ^a  

^a MONTANA STATE UNIVERSITY   (United States)

^b MICHIGAN STATE UNIVERSITY   (United States)

^c EMORY UNIVERSITY   (United States)

^d CEA GRENOBLE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AEROBIC INCUBATION; AEROBIC INDUCTIONS; ANAEROBIC CONDITIONS; ANAEROBIC INCUBATION; CLUSTER STATE; DEOXYADENOSINE; IN-VITRO; IN-VIVO; INTERCONVERSIONS; IRON SPECIES; IRON-SULFUR CLUSTERS; LOCALIZED STATE; OXIDATIVE DAMAGE; OXYGEN LEVELS; PURIFIED ENZYME; PYRUVATES; REDOX STATE; SMALL MOLECULES; TOTAL IRONS; WHOLE CELL;

CELL CULTURE; CELL MEMBRANES; ENZYMES; MOLYBDENUM; OXYGEN; PURIFICATION; SULFUR;

ACOUSTIC EMISSIONS;

5' DEOXYADENOSINE; 5' METHYLTHIOADENOSINE PHOSPHORYLASE; ADENOSINE DERIVATIVE; ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ENZYME; FERRIC ION; FERROUS ION; FORMATE ACETYLTRANSFERASE ACTIVATING ENZYME; FORMIC ACID; IRON SULFUR PROTEIN; LYASE; PYRUVIC ACID; UNCLASSIFIED DRUG;

ARTICLE; CELL CULTURE; CLUSTER ANALYSIS; ENZYME ACTIVATION; ENZYME PURIFICATION; INCUBATION TIME; MOLECULE; MOSSBAUER SPECTROSCOPY; NONHUMAN; OXIDATION REDUCTION STATE; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN EXPRESSION; WHOLE CELL;

ELECTRONS; ENZYME ACTIVATION; ENZYMES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FERRIC COMPOUNDS; FERROUS COMPOUNDS; GENE EXPRESSION REGULATION, BACTERIAL; IRON-SULFUR PROTEINS; SPECTROSCOPY, MOSSBAUER;

EID: 70349632868     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9010286     Document Type: Article

References (28)

1. Sawers, G., and Bock, A. (1988) Anaerobic regulation of pyruvate formate-lyase from Escherichia coli K12. J. Bacteriol. 170, 5330-5336.
2. Sawers, G., and Bock, A. (1989) Novel transcriptional control of the pyruvate formate-lyase gene: upstream regulatory sequences and multiple promoters regulate anaerobic expression. J. Bacteriol. 171, 2485-2498.
3. Sawers, G., and Summpann, B. (1992) Anaerobic induction of pyruvate formate-lyase gene expression is mediated by the ArcA and FNR proteins. J. Bacteriol. 174, 3474-3478.
4. Knappe, J., Neugebauer, F. A., Blaschkowski, H. P., and Gänzler, M. (1984) Post-translational activation introduces a free radical into pyruvate formate-lyase. Proc. Natl. Acad. Sci U.S.A. 81, 1332-1335.
5. Wagner, A. F. V., Frey, M., Neugebauer, F. A., Schäfer, W., and Knappe, J. (1992) The free radical in pyruvate formate-lyase is located on glycine-734. Proc. Natl. Acad. Sci. U.S.A. 89, 996-1000.
6. Buckel, W., and Golding, B. T. (2006) Radical enzymes in anaerobes. Annu. Rev. Microbiol. 60, 27-49.
7. Sofia, H. J., Chen, G., Hetzler, B. G., Reyes-Spindola, J. F., and Miller, N. E. (2001) RadicalSAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res. 29, 1097-1106. (Pubitemid 32186195)
8. Rödel, W., Plaga, W., Frank, R., and Knappe, J. (1988) Primary structures of Escherichia coli pyruvate formate-lyase and pyruvate formate-lyase-activating enzyme deduced from the DNA nucleotide sequences. Eur. J. Biochem. 177, 153-158.
9. Külzer, R., Pils, T., Kappl, R., Hüttermann, J., and Knappe, J. (1998) Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme. Molecular properties of the holoenzyme form. J. Biol. Chem. 273, 4897-4903.
10. Krebs, C., Broderick, W. E., Henshaw, T. F., Broderick, J. B., and Huynh, B. H. (2002) Coordination of adenosylmethionine to a unique iron site of the [4Fe-4S] of pyruvate formate-lyase activating enzyme: A Mössbauer spectroscopic study. J. Am. Chem. Soc. 124, 912-913.
11. Walsby, C. J., Ortillo, D., Broderick, W. E., Broderick, J. B., and Hoffman, B. M. (2002) An anchoring role for FeS Clusters: Chelation of the amino acid moiety of S-adenosylmethionine to the unique iron site of the [4Fe-4S] cluster of pyruvate formate-lyase activating enzyme. J. Am. Chem. Soc. 124, 11270-11271.
12. Walsby, C., Ortillo, D., Yang, J., Nnyepi, M., Broderick, W. E., Hoffman, B. M., and Broderick, J. B. (2005) Spectroscopic approaches to elucidating novel iron-sulfur chemistry in the "Radical SAM" protein superfamily. Inorg. Chem. 44, 727-741.
13. Vey, J. L., Yang, J., Li, M., Broderick, W. E., Broderick, J. B., and Drennan, C. L. (2008) Structural basis for glycyl radical formation by pyruvate formate-lyase activating enzyme. Proc. Natl. Acad. Sci. U.S. A. 105, 16137-16141.
14. + cluster of pyruvate formate-lyase activating enzyme. J. Am. Chem. Soc. 124, 3143-3151.
15. + cluster of pyruvate formate-lyase activating enzyme generates the glycyl radical on pyruvate formate-lyase: EPR-detected single turnover. J. Am. Chem. Soc. 122, 8331-8332.
16. Knappe, J., and Sawers, G. (1990) A radical-chemical route to acetyl- CoA: the anaerobically induced pyruvate formate-lyase system of Escherichia coli. FEMS Microbiol. Rev. 75, 383-398.
17. Sauter, M., and Sawers, R. G. (1990) Transcriptional analysis of the gene encoding pyruvate formate-lyase-activating enzyme of Escherichia coli. Mol. Microbiol. 4, 355-363.
18. Knappe, J., Blaschkowski, H. P., Gröbner, P., and Schmitt, T. (1974) Pyruvate formate-lyase of Escherichia coli: the acetyl-enzyme intermediate. Eur. J. Biochem. 50, 253-263.
19. Broderick, J. B., Duderstadt, R. E., Fernandez, D. C., Wojtuszewski, K., Henshaw, T. F., and Johnson, M. K. (1997) Pyruvate formatelyase activating enzyme is an iron-sulfur protein. J. Am. Chem. Soc. 119, 7396-7397.
20. Broderick, J. B., Henshaw, T. F., Cheek, J., Wojtuszewski, K., Smith, S. R., Trojan, M. R., McGhan, R. M., Kopf, A., Kibbey, M., and Broderick, W. E. (2000) Pyruvate formate-lyase activating enzyme: strictly anaerobic isolation yields active enzyme containing a [3Fe- 4S]+ cluster. Biochem. Biophys. Res. Commun. 269, 451-456. (Pubitemid 30440321)
21. Krebs, C., Henshaw, T. F., Cheek, J., Huynh, B.-H., and Broderick, J. B. (2000) Conversion of 3Fe-4S to 4Fe-4S clusters in native pyruvate formate lyase activating enzyme: Mössbauer characterization and implications for mechanism. J. Am. Chem. Soc. 122, 12497-12506.
22. Popescu, C. V., Bates, D. M., Beinert, H., Münck, E., and Kiley, P. J. (1998) Mössbauer spectroscopy as a tool for the study of activation/ inactivation of the transcription regulator FNR in whole cells of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 95, 13431-13435.
23. Benda, R., Bui, B. T. S., Schünemann, V., Florentin, D., Marquet, A., and Trautwein, A. X. (2002) Iron-sulfur clusters of biotin synthase in vivo: a Mössbauer study. Biochemistry 41, 15000-15006. (Pubitemid 35470679)
24. 2+ protein in whole cells. FEBS Lett. 529, 332-336.
25. Matzanke, B. F., Müller, G. I., Bill, E., and Trautwein, A. X. (1989) Iron metabolism of Escherichia coli studied by Mössbauer spectroscopy and biochemical methods. Eur. J. Biochem. 183, 371-379.
26. Ayala-Castro, C., Saini, A., and Outten, F. W. (2008) Fe-S cluster assembly pathways in bacteria. Microbiol. Mol. Biol. Rev. 72, 110-125.
27. Trautwein, A. X., Bill, E., Bominaar, E. L., and Winkler, H. (1991) Iron-containing proteins and related analogs - complementary Mössbauer, EPR, and magnetic susceptibility studies. Struct. Bonding (Berlin) 78, 1-95.
28. 4] cluster chemistry in ferredoxin:thioredoxin reductase: implications for the catalytic mechanism. J. Am. Chem. Soc. 127, 9612-9624.