SEARCH

SEARCH BY CITATION

References

  • Alen, C., Sonenshein, A.L. (1999) Bacillus subtilis aconitase is an RNA-binding protein. Proc Natl Acad Sci USA 96: 1041210417.
  • Babini, E., Borsari, M., Capozzi, F., Eltis, L.D., Luchinat, C. (1999) Experimental evidence for the role of buried polar groups in determining the reduction potential of metalloproteins: the S79P variant of Chromatium vinosum HiPIP. J Biol Inorg Chem 4: 692700.
  • Benov, L., Fridovich, I. (1999) Why superoxide imposes an aromatic amino acid auxotrophy on Escherichia coli. The transketolase connection. J Biol Chem 274: 42024206.
  • Berkovitch, F., Nicolet, Y., Wan, J.T., Jarrett, J.T., Drennan, C.L. (2004) Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science 303: 7679.
  • Bertini, I., Cowan, J.A., Luchinat, C., Natarajan, K., Piccioli, M. (1997) Characterization of a partially unfolded high potential iron protein. Biochemistry 36: 93329339.
  • Bjerrum, C.J., Canfield, D.E. (2002) Ocean productivity before about 1.9 Gyr ago limited by phosphorus adsorption onto iron oxides. Nature 417: 159162.
  • Boehme, D.E., Vincent, K., Brown, O.R. (1976) Oxygen and toxicity: inhibition of amino acid biosynthesis. Nature 262: 418420.
  • Bossi, R.T., Negri, A., Tedeschi, G., Mattevi, A. (2002) Structure of FAD-bound l-aspartate oxidase: insight into substrate specificity and catalysis. Biochemistry 41: 30183024.
  • Brickman, T.J., McIntosh, M.A. (1992) Overexpression and purification of ferric enterobactin esterase from Escherichia coli. Demonstration of enzymatic hydrolysis of enterobactin and its iron complex. J Biol Chem 267: 1235012355.
  • Canfield, D.E., Habicht, K.S., Thamdrup, B. (2000) The archean sulfur cycle and the early history of atmospheric oxygen. Science 288: 658661.
  • Capozzi, F., Ciurli, S., Luchinat, C. (1998) Coordination sphere versus protein environment as determinants of electronic and functional properties of iron-sulfur proteins. Struct Bonding 90: 127160.
  • Carlioz, A., Touati, D. (1986) Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life? EMBO J 5: 623630.
  • Chabriere, E., Charon, M.H., Volbeda, A., Pieulle, L., Hatchikian, E.C., Fontecilla-Camps, J.C. (1999) Crystal structures of the key anaerobic enzyme pyruvate: ferredoxin oxidoreductase, free and in complex with pyruvate. Nat Struct Biol 6: 182190.
  • Chen, D., Walsby, C., Hoffman, B.M., Frey, P.A. (2003) Coordination and mechanism of reversible cleavage of S-adenosylmethionine by the [4Fe-4S] center in lysine 2,3-aminomutase. J Am Chem Soc 125: 1178811789.
  • Ding, H., Demple, B. (1997) In vivo kinetics of a redox-regulated transcriptional switch. Proc Natl Acad Sci USA 94: 84458449.
  • Eibbe, M., Gadkari, D., Meyer, O. (1997) N2 fixation by Streptomyces thermoautotrophicus involves a molybdenum-dinitrogenase and a manganese-superoxide oxidoreductase that couple N2 reduction to the oxidation of superoxide produced from O2 by a molybdenum-CO dehydrogenase. J Biol Chem 272: 2662726633.
  • Flint, D.H., Emptage, M.H. (1990) Dihydroxyacid dehydratase: isolation, characterization as Fe-S proteins, and sensitivity to inactivation by oxygen radicals. In Biosynthesis of Branched Chain Amino Acids. Barak, Z., Chipman, D., Schloss, J.V. (eds). New York: VCH Publishers, pp. 285314.
  • Flint, D.H., Tuminello, J.F., Emptage, M.H. (1993) The inactivation of Fe-S cluster containing hydro-lyases by superoxide. J Biol Chem 268: 2236922376.
  • Flo, T.H., Smith, K.D., Sato, S., Rodriguez, D.J., Holmes, M.A., Strong, R.K., et al. (2004) Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron. Nature 432: 917921.
  • Frey, M. (2002) Hydrogenases: hydrogen-activating enzymes. Chembiochem 2002: 153160.
  • Gardner, P.R., Fridovich, I. (1991) Superoxide sensitivity of the Escherichia coli aconitase. J Biol Chem 266: 1932819333.
  • Gaudu, P., Moon, N., Weiss, B. (1997) Regulation of the soxRS oxidative stress regulon. Reversible oxidation of the Fe-S center of SoxR in vivo. J Biol Chem 272: 50825086.
  • Goldstein, S., Meyerstein, D., Czapski, G. (1993) The Fenton reagents. Free Rad Biol Med 15: 435445.
  • Golinelli, M.-P., Chatelet, C., Duin, E.C., Johnson, M.K., Meyer, J. (1998) Extensive ligand rearrangements around the [2Fe-2S] cluster of Clostridium pasteurianum ferredoxin. Biochemistry 37: 1042910437.
  • Gort, A.S., Imlay, J.A. (1998) Balance between endogenous superoxide stress and antioxidant defenses. J Bacteriol 180: 14021410.
  • Grimek, T.L., Escalante-Semerena, J.C. (2004) The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a new Fe-S-dependent 2-methylcitrate dehydratase enzyme that requires prpF function in vivo. J Bacteriol 186: 454462.
  • Gruer, M.J., Guest. J.R. (1994) Two genetically-distinct and differentially-regulated aconitases (AcnA and AcnB) in Escherichia coli. Microbiology 140: 25312541.
  • Helmann, J.D., Wu, M.F., Gaballa, A., Kobel, P.A., Morshedi, M.M., Fawcett, P., Paddon, C. (2003) The global transcriptional response of Bacillus subtilis to peroxide stress is coordinated by three transcription factors. J Bacteriol 185: 243253.
  • Inbaraj, J.J., Chignell, C.F. (2004) Cytotoxic action of juglone and plumbagin: a mechanistic study using HaCaT keratinocytes. Chem Res Toxicol 17: 5562.
  • Iverson, T.M., Luna-Chavez, C., Cecchini, G., Rees. D.C. (1999) Structure of the Escherichia coli fumarate reductase respiratory complex. Science 284: 19611966.
  • Jarrett, J.T. (2005) The novel structure and chemistry of iron-sulfur clusters in the adenosylmenthionine-dependent radical enzyme biotin synthase. Arch Biochim Biophys 433: 312321.
  • Jenney, F.E., Jr, Verhagen, M.F.J.M., Cui, X., Adams, M.W.W. (1999) Anaerobic microbes: oxygen detoxification without superoxide dismutase. Science 286: 306309.
  • Johnson, D., Dean, D.R., Smith, A.D., Johnson, M.K. (2005) Structure, function, and formation of biological iron-sulfur clusters. Ann Rev Biochem 74: 247281.
  • Kaptain, S., Downey, W.E., Tang, C., Philpott, C., Haile, D., Orloff, D.G., et al. (1991) A regulated RNA binding protein also possesses aconitase activity. Proc Natl Acad Sci USA 88: 1010910113.
  • Keyer, K., Imlay, J.A. (1996) Superoxide accelerates DNA damage by elevating free-iron levels. Proc Natl Acad Sci USA 93: 1363513640.
  • Khoroshilova, N., Popescu, C., Munck, E., Beinert, H., Kiley, P. (1997) Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by O2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity. Proc Natl Acad Sci USA 94: 60876092.
  • Kim, J., Hetzel, M., Boiangiu, C.D., Buckel, W. (2004) Dehydration of (R)-2-hydroxyacyl-CoA to enoyl-CoA in the fermentation of α-amino acids by anaerobic bacteria. FEMS Micro Rev 28: 455468.
  • Kuo, C.F., Mashino, T., Fridovich, I. (1987) α,β-dihydroxyisovalerate dehydratase: a superoxide-sensitive enzyme. J Biol Chem 262: 47244727.
  • Lauble, H., Kennedy, M.C., Beinert, H., Stout, C.D. (1992) Crystal structures of aconitase with isocitrate and nitroisocitrate bound. Biochemistry 31: 27352748.
  • Layer, G., Moser, J., Heinz, D.W., Jahn, D., Schubert, W.-D. (2003) Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical SAM enzymes. EMBO J 22: 62146224.
  • Liochev, S.I., Fridovich, I. (1992) Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon. Proc Natl Acad Sci USA 89: 58925896.
  • Liochev, S.I., Fridovich, I. (1994) The role of superoxide in the production of hydroxyl radical: in vitro and in vivo. Free Rad Biol Med 16: 2933.
  • Lombard, M., Fontecave, M., Touati, D., Niviere, V. (2000) Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity. J Biol Chem 275: 115121.
  • McHugh, J.P., Rodrigues-Quinones, F., Abdul-Tehrani, H., Svistunenko, D.A., Poole, R.K., Cooper, C.E., Andrews, S.C. (2003) Global iron-dependent gene regulation in Escherichia coli. J Biol Chem 278: 2947829486.
  • Martins, B.M., Dobbek, H., Cinkaya, I., Buckel, W., Messerschmidt, A. (2004) Crystal structure of 4-hydroxybutyryl-CoA dehydratase: radical catalysis involving a [4Fe-4S] cluster and flavin. Proc Natl Acad Sci USA 101: 1564515649.
  • Masse, E., Gottesman, S. (2002) A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc Natl Acad Sci USA 99: 46204625.
  • Naqui, A., Chance, B. (1986) Reactive oxygen intermediates in biochemistry. Annu Rev Biochem 55: 137166.
  • Neilands, J.B. (1993) Siderophores. Arch Biochem Biophys 302: 13.
  • Outten, C.E., O'Halloran, T.V. (2001) Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science 292: 24882492.
  • Outten, F.W., Djaman, O., Storz. G. (2004) A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli. Mol Microbiol 52: 861872.
  • Page, C.C., Moser, C.C., Dutton, P.L. (2003) Mechanism for electron transfer within and between proteins. Curr Opin Chem Biol 7: 551556.
  • Pan, N., Imlay, J.A. (2001) How does oxygen inhibit central metabolism in the obligate anaerobe Bacteroides thetaiotaomicron? Mol Microbiol 39: 15621571.
  • Park, S., You, X., Imlay, J.A. (2005) Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx mutants of Escherichia coli. Proc Natl Acad Sci USA 102: 93179322.
  • Peters, J.W., Lanzilotta, W.N., Lemon, B.J., Seefeldt, L.C. (1998) X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom resolution. Science 282: 18531858.
  • Pieulle, L., Magro, V., Hatchikian, E.C. (1997) Isolation and analysis of the gene encoding the pyruvate-ferredoxin oxidoreductase of Desulfovibrio africanus, production of the recombinant enzyme in Escherichia coli, and effect of carboxy-terminal deletions on its stability. J Bacteriol 179: 56845692.
  • Plank, D.W., Kennedy, M.C., Beinert, H., Howard, J.B. (1989) Cysteine labeling studies of beef heart aconitase containing a 4Fe, a cubane 3Fe, or a linear 3Fe cluster. J Biol Chem 264: 2038520393.
  • Puig, S., Askeland, F., Thiele, D.J. (2005) Coordinated remodeling of cellular metabolism during iron deficiency through targeted mRNA degradation. Cell 120: 99110.
  • Ran, H., Hassett, D.J., Lau, G.W. (2003) Human targets of Pseudomonas aeruginosa pyocyanin. Proc Natl Acad Sci USA 100: 1431514320.
  • Rao, P.V., Holm, R.H. (2004) Synthetic analogues of the active sites of iron-sulfur proteins. Chem Rev 104: 527559.
  • Rees, D.C. (2002) Great metalloclusters in enzymology. Ann Rev Biochem 71: 221246.
  • Seaver, L.C., Imlay, J.A. (2001) Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli. J Bacteriol 183: 71827189.
  • Tang, Y., Guest, J.R. (1999) Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases. Microbiology 145: 30693079.
  • Tokumoto, U., Kitamura, S., Fukuyama, K., Takahashi, Y. (2004) Interchageability and distinct properties of bacterial Fe-S cluster assembly systems: functional replacement of the isc and suf operons in Escherichia coli with the nifSU-like operon from Helicobacter pylori. J Biochem (Tokyo) 136: 199209.
  • Varghese, S.M., Tang, Y., Imlay, J.A. (2003) Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion. J Bacteriol 185: 221230.
  • Wandersman, C., Delepelaire, P. (2004) Bacterial iron sources: from siderophores to hemophores. Ann Rev Microbiol 58: 611647.
  • Ward, P.P., Conneely, O.M. (2004) Lactoferrin: role in iron homeostasis and host defense against microbial infection. Biometals 17: 203208.
  • Wiener, M.C. (2005) TonB-dependent outer membrane transport: going for Baroque? Curr Opin Struct Biol 15: 294400.
  • Yankovskaya, V., Horsefield, R., Tornroth, S., Luna-Chavez, C., Miyoshi, H., Leger, C., et al. (2003) Architecture of succinate dehydrogenase and reactive oxygen species generation. Science 299: 700704.
  • Zheng, M., Wang, X., Templeton, L.J., Smulski, D.R., LaRossa, R.A., Storz, G. (2001) DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide. J Bacteriol 183: 45624570.