메뉴 건너뛰기




Volumn 48, Issue 2, 2010, Pages 292-297

Dps proteins prevent Fenton-mediated oxidative damage by trapping hydroxyl radicals within the protein shell

Author keywords

DNA protection; Dps proteins; Fenton chemistry; Free radicals; Hydroxyl radicals; Intraprotein radicals

Indexed keywords

DPS PROTEIN; HYDROGEN PEROXIDE; HYDROXYL RADICAL; TRYPTOPHAN; TYROSINE;

EID: 72649096714     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2009.10.053     Document Type: Article
Times cited : (50)

References (45)
  • 2
    • 0034912671 scopus 로고    scopus 로고
    • Radical mechanisms of enzymatic catalysis
    • Frey P.A. Radical mechanisms of enzymatic catalysis. Annu. Rev. Biochem. 70 (2001) 121-148
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 121-148
    • Frey, P.A.1
  • 3
    • 1442328094 scopus 로고    scopus 로고
    • Electron tunnelling through proteins
    • Gray H.B., and Winkler J.R. Electron tunnelling through proteins. Q. Rev. Biophys. 36 (2003) 341-372
    • (2003) Q. Rev. Biophys. , vol.36 , pp. 341-372
    • Gray, H.B.1    Winkler, J.R.2
  • 4
    • 0142231009 scopus 로고    scopus 로고
    • Mechanism for electron transfer within and between proteins
    • Page C.C., Moser C.C., and Dutton L.P. Mechanism for electron transfer within and between proteins. Curr. Opin. Chem. Biol. 7 (2003) 551-556
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 551-556
    • Page, C.C.1    Moser, C.C.2    Dutton, L.P.3
  • 5
    • 34249992893 scopus 로고    scopus 로고
    • Protein electron transfer (mechanism and reproductive toxicity): iminium, hydrogen bonding, homoconjugation, amino acid side chains (redox and charged), and cell signaling
    • Kovacic P. Protein electron transfer (mechanism and reproductive toxicity): iminium, hydrogen bonding, homoconjugation, amino acid side chains (redox and charged), and cell signaling. Birth Defects Res. 81 (2007) 51-54
    • (2007) Birth Defects Res. , vol.81 , pp. 51-54
    • Kovacic, P.1
  • 7
    • 63049099068 scopus 로고    scopus 로고
    • Electron transfer in peptides and proteins
    • Cordes M., and Giese B. Electron transfer in peptides and proteins. Chem. Soc. Rev. 38 (2009) 892-901
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 892-901
    • Cordes, M.1    Giese, B.2
  • 8
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay J.A. Pathways of oxidative damage. Annu. Rev. Microbiol. 57 (2003) 395-418
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 9
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide. Annu. Rev
    • Imlay J.A. Cellular defenses against superoxide and hydrogen peroxide. Annu. Rev. Microbiol 77 (2008) 755-776
    • (2008) Microbiol , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 10
    • 0037101879 scopus 로고    scopus 로고
    • Ferritin, iron homeostasis, and oxidative damage
    • Arosio P., and Levi S. Ferritin, iron homeostasis, and oxidative damage. Free Radic. Biol. Med. 33 (2002) 457-463
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 457-463
    • Arosio, P.1    Levi, S.2
  • 11
    • 67349100157 scopus 로고    scopus 로고
    • Ferritins: a family of molecules for iron storage, antioxidation and more
    • Arosio P., Ingrassia R., and Cavadini P. Ferritins: a family of molecules for iron storage, antioxidation and more. Biochim. Biophys. Acta 1790 (2009) 589-599
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 589-599
    • Arosio, P.1    Ingrassia, R.2    Cavadini, P.3
  • 12
    • 0037008743 scopus 로고    scopus 로고
    • Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells: a ferritin-like DNA-binding protein of Escherichia coli
    • Zhao G., Ceci P., Ilari A., Giangiacomo L., Laue T.M., Chiancone E., and Chasteen N.D. Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells: a ferritin-like DNA-binding protein of Escherichia coli. J. Biol. Chem. 277 (2002) 27689-27696
    • (2002) J. Biol. Chem. , vol.277 , pp. 27689-27696
    • Zhao, G.1    Ceci, P.2    Ilari, A.3    Giangiacomo, L.4    Laue, T.M.5    Chiancone, E.6    Chasteen, N.D.7
  • 15
    • 0031029483 scopus 로고    scopus 로고
    • Dinuclear center of ferritin: studies of iron binding and oxidation show differences in the two iron sites
    • Treffry A., Zhao Z., Quail M.A., Guest J.R., and Harrison P.M. Dinuclear center of ferritin: studies of iron binding and oxidation show differences in the two iron sites. Biochemistry 36 (1997) 432-441
    • (1997) Biochemistry , vol.36 , pp. 432-441
    • Treffry, A.1    Zhao, Z.2    Quail, M.A.3    Guest, J.R.4    Harrison, P.M.5
  • 17
    • 0033986734 scopus 로고    scopus 로고
    • The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron binding site
    • Ilari A., Stefanini S., Chiancone E., and Tsernoglou D. The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron binding site. Nat. Struct. Biol. 7 (2000) 38-43
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 38-43
    • Ilari, A.1    Stefanini, S.2    Chiancone, E.3    Tsernoglou, D.4
  • 18
    • 0031959912 scopus 로고    scopus 로고
    • The crystal structure of Dps, a ferritin homolog that binds and protects DNA
    • Grant R.A., Filman D.J., Finkel S.E., Kolter R., and Hogle J.M. The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nat. Struct. Biol. 5 (1998) 294-303
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 294-303
    • Grant, R.A.1    Filman, D.J.2    Finkel, S.E.3    Kolter, R.4    Hogle, J.M.5
  • 19
    • 0034254215 scopus 로고    scopus 로고
    • Iron oxidation and hydrolysis reactions of a novel ferritin from Listeria innocua
    • Yang X., Chiancone E., Stefanini S., Ilari A., and Chasteen N.D. Iron oxidation and hydrolysis reactions of a novel ferritin from Listeria innocua. Biochem. J. 349 (2000) 783-786
    • (2000) Biochem. J. , vol.349 , pp. 783-786
    • Yang, X.1    Chiancone, E.2    Stefanini, S.3    Ilari, A.4    Chasteen, N.D.5
  • 20
    • 17144402211 scopus 로고    scopus 로고
    • The so-called Listeria innocua ferritin is a Dps protein: iron incorporation, detoxification, and DNA protection properties
    • Su M., Cavallo S., Stefanini S., Chiancone E., and Chasteen N.D. The so-called Listeria innocua ferritin is a Dps protein: iron incorporation, detoxification, and DNA protection properties. Biochemistry 44 (2005) 5572-5578
    • (2005) Biochemistry , vol.44 , pp. 5572-5578
    • Su, M.1    Cavallo, S.2    Stefanini, S.3    Chiancone, E.4    Chasteen, N.D.5
  • 21
    • 17144367329 scopus 로고    scopus 로고
    • The unusual intersubunit ferroxidase center of Listeria innocua Dps is required for hydrogen peroxide detoxification but not for iron uptake: a study with site-specific mutants
    • Ilari A., Latella M.C., Ceci P., Ribacchi F., Su M., Giangiacomo L., Stefanini S., Chasteen N.D., and Chiancone E. The unusual intersubunit ferroxidase center of Listeria innocua Dps is required for hydrogen peroxide detoxification but not for iron uptake: a study with site-specific mutants. Biochemistry 44 (2005) 5579-5587
    • (2005) Biochemistry , vol.44 , pp. 5579-5587
    • Ilari, A.1    Latella, M.C.2    Ceci, P.3    Ribacchi, F.4    Su, M.5    Giangiacomo, L.6    Stefanini, S.7    Chasteen, N.D.8    Chiancone, E.9
  • 22
    • 23744476494 scopus 로고    scopus 로고
    • Dps/Dpr ferritin-like protein: insight into the mechanism of iron incorporation and evidence for a central role in cellular iron homeostasis in Streptococcus suis
    • Pulliainen A.T., Kauko A., Haataja S., Papageorgiou A.C., and Finne J. Dps/Dpr ferritin-like protein: insight into the mechanism of iron incorporation and evidence for a central role in cellular iron homeostasis in Streptococcus suis. Mol. Microbiol. 57 (2005) 1086-1100
    • (2005) Mol. Microbiol. , vol.57 , pp. 1086-1100
    • Pulliainen, A.T.1    Kauko, A.2    Haataja, S.3    Papageorgiou, A.C.4    Finne, J.5
  • 23
    • 33751057232 scopus 로고    scopus 로고
    • Iron incorporation in Streptococcus suis Dps-like peroxide resistance protein Dpr requires mobility in the ferroxidase center and leads to formation of a ferrihydrite-like core
    • Kauko A., Pulliainen A.T., Haataja S., Meyer-Klaucke W., Finne J., and Papageorgiou A.C. Iron incorporation in Streptococcus suis Dps-like peroxide resistance protein Dpr requires mobility in the ferroxidase center and leads to formation of a ferrihydrite-like core. J. Mol. Biol. 364 (2006) 97-109
    • (2006) J. Mol. Biol. , vol.364 , pp. 97-109
    • Kauko, A.1    Pulliainen, A.T.2    Haataja, S.3    Meyer-Klaucke, W.4    Finne, J.5    Papageorgiou, A.C.6
  • 24
    • 33748878031 scopus 로고    scopus 로고
    • Paired Bacillus anthracis Dps (mini-ferritin) have different reactivities with peroxide
    • Liu X., Kim K., Leighton T., and Theil E.C. Paired Bacillus anthracis Dps (mini-ferritin) have different reactivities with peroxide. J. Biol. Chem. 281 (2006) 27827-27835
    • (2006) J. Biol. Chem. , vol.281 , pp. 27827-27835
    • Liu, X.1    Kim, K.2    Leighton, T.3    Theil, E.C.4
  • 25
    • 0020541188 scopus 로고
    • Ribonucleotide reductase-a radical enzyme
    • Reichard P., and Eherenberg A. Ribonucleotide reductase-a radical enzyme. Science 221 (1983) 514-519
    • (1983) Science , vol.221 , pp. 514-519
    • Reichard, P.1    Eherenberg, A.2
  • 26
    • 0031849153 scopus 로고    scopus 로고
    • Ribonucleotide reductase and radical reactions
    • Fontecave M. Ribonucleotide reductase and radical reactions. Cell. Mol. Life Sci. 54 (1998) 684-695
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 684-695
    • Fontecave, M.1
  • 27
    • 0034645606 scopus 로고    scopus 로고
    • Mechanism of rapid electron transfer during oxygen activation in the R2 subunit of Escherichia coli ribonucleotide reductase. 1. Evidence for a transient tryptophan radical
    • Baldwin J., Krebs C., Ley B.A., Edmondson D.E., Huynh B.H., and Bollinger Jr. J.M. Mechanism of rapid electron transfer during oxygen activation in the R2 subunit of Escherichia coli ribonucleotide reductase. 1. Evidence for a transient tryptophan radical. J. Am. Chem. Soc. 122 (2000) 12195-12206
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12195-12206
    • Baldwin, J.1    Krebs, C.2    Ley, B.A.3    Edmondson, D.E.4    Huynh, B.H.5    Bollinger Jr., J.M.6
  • 28
    • 0034645585 scopus 로고    scopus 로고
    • Mechanism of rapid electron transfer during oxygen activation in the R2 subunit of Escherichia coli ribonucleotide reductase. 2. Evidence for and consequences of blocked electron transfer in the W48F variant
    • Krebs C., Chen S., Baldwin J., Ley B.A., Patel U., Edmondson D.E., Huynh B.H., and Bollinger Jr. J.M. Mechanism of rapid electron transfer during oxygen activation in the R2 subunit of Escherichia coli ribonucleotide reductase. 2. Evidence for and consequences of blocked electron transfer in the W48F variant. J. Am. Chem. Soc. 122 (2000) 12207-12219
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12207-12219
    • Krebs, C.1    Chen, S.2    Baldwin, J.3    Ley, B.A.4    Patel, U.5    Edmondson, D.E.6    Huynh, B.H.7    Bollinger Jr., J.M.8
  • 29
    • 34547462698 scopus 로고    scopus 로고
    • Spectroscopic and electronic structure studies of intermediate X in ribonucleotide reductase R2 and two variants: a description of the FeIV-Oxo bond in the FeIII-O-FeIV dimer
    • Mitić N., Clay M.D., Saleh L., Bollinger J.M., and Solomon E.I. Spectroscopic and electronic structure studies of intermediate X in ribonucleotide reductase R2 and two variants: a description of the FeIV-Oxo bond in the FeIII-O-FeIV dimer. J. Am. Chem. Soc. 129 (2007) 9049-9065
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 9049-9065
    • Mitić, N.1    Clay, M.D.2    Saleh, L.3    Bollinger, J.M.4    Solomon, E.I.5
  • 30
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., and von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182 (1989) 319-326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 32
    • 0041322950 scopus 로고    scopus 로고
    • Re-evaluation of intramolecular long-range electron transfer between tyrosine and tryptophan in lysozymes: evidence for the participation of other residues
    • Stuart-Audette M., Blouquit Y., Faraggi M., Sicard-Roselli C., Houé-Levin C., and Jollès P. Re-evaluation of intramolecular long-range electron transfer between tyrosine and tryptophan in lysozymes: evidence for the participation of other residues. Eur. J. Biochem. 270 (2003) 3565-3571
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3565-3571
    • Stuart-Audette, M.1    Blouquit, Y.2    Faraggi, M.3    Sicard-Roselli, C.4    Houé-Levin, C.5    Jollès, P.6
  • 33
    • 0027083350 scopus 로고
    • A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli
    • Almirón M., Link A.J., Furlong D., and Kolter R. A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev. 6 (1992) 2646-2654
    • (1992) Genes Dev. , vol.6 , pp. 2646-2654
    • Almirón, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 34
    • 0031032646 scopus 로고    scopus 로고
    • A novel non-heme iron binding ferritin related to the DNA-binding proteins of the Dps family in Listeria innocua
    • Bozzi M., Mignogna G., Stefanini S., Barra D., Longhi C., Valenti P., and Chiancone E. A novel non-heme iron binding ferritin related to the DNA-binding proteins of the Dps family in Listeria innocua. J. Biol. Chem. 272 (1997) 3259-3265
    • (1997) J. Biol. Chem. , vol.272 , pp. 3259-3265
    • Bozzi, M.1    Mignogna, G.2    Stefanini, S.3    Barra, D.4    Longhi, C.5    Valenti, P.6    Chiancone, E.7
  • 36
    • 0031735117 scopus 로고    scopus 로고
    • Long-lived charge-separated species observed on flash photolysis of peptides conjugates: interplay of local and radical ion pair triplet states
    • Jones G., and Lu N.J. Long-lived charge-separated species observed on flash photolysis of peptides conjugates: interplay of local and radical ion pair triplet states. Org. Chem. 63 (1998) 8938-8945
    • (1998) Org. Chem. , vol.63 , pp. 8938-8945
    • Jones, G.1    Lu, N.J.2
  • 37
    • 0037928595 scopus 로고    scopus 로고
    • The iron-oxygen reconstitution reaction in protein R2-Tyr-177 mutants of mouse ribonucleotide reductase: EPR and electron nuclear double resonance studies on a new transient tryptophan radical
    • Pötsch S., Lendzian F., Ingemarson R., Hörnberg A., Thelander L., Lubitz W., Lassmann G., and Gräslund A. The iron-oxygen reconstitution reaction in protein R2-Tyr-177 mutants of mouse ribonucleotide reductase: EPR and electron nuclear double resonance studies on a new transient tryptophan radical. J. Biol. Chem. 274 (1999) 17696-17704
    • (1999) J. Biol. Chem. , vol.274 , pp. 17696-17704
    • Pötsch, S.1    Lendzian, F.2    Ingemarson, R.3    Hörnberg, A.4    Thelander, L.5    Lubitz, W.6    Lassmann, G.7    Gräslund, A.8
  • 40
    • 33847067891 scopus 로고    scopus 로고
    • The mutations Lys 114 → Gln and Asp 126 → Asn disrupt an intersubunit salt bridge and convert Listeria innocua Dps into its natural mutant Listeria monocytogenes Dps: effects on protein stability at low pH
    • Bellapadrona G., Chiaraluce R., Consalvi V., Ilari A., Stefanini S., and Chiancone E. The mutations Lys 114 → Gln and Asp 126 → Asn disrupt an intersubunit salt bridge and convert Listeria innocua Dps into its natural mutant Listeria monocytogenes Dps: effects on protein stability at low pH. Proteins 66 (2007) 975-983
    • (2007) Proteins , vol.66 , pp. 975-983
    • Bellapadrona, G.1    Chiaraluce, R.2    Consalvi, V.3    Ilari, A.4    Stefanini, S.5    Chiancone, E.6
  • 41
    • 34249846924 scopus 로고    scopus 로고
    • The neutrophil-activating Dps protein of Helicobacter pylori, HP-NAP, adopts a mechanism different from Escherichia coli Dps to bind and condense DNA
    • Ceci P., Mangiarotti L., Rivetti C., and Chiancone E. The neutrophil-activating Dps protein of Helicobacter pylori, HP-NAP, adopts a mechanism different from Escherichia coli Dps to bind and condense DNA. Nucleic Acids Res. 35 (2007) 2247-2256
    • (2007) Nucleic Acids Res. , vol.35 , pp. 2247-2256
    • Ceci, P.1    Mangiarotti, L.2    Rivetti, C.3    Chiancone, E.4
  • 42
    • 0034214080 scopus 로고    scopus 로고
    • Intraprotein radical transfer during photoactivation of DNA photolyase
    • Aubert C., Vos M.H., Mathis P., Eker A.P., and Brettel K. Intraprotein radical transfer during photoactivation of DNA photolyase. Nature 405 (2000) 586-590
    • (2000) Nature , vol.405 , pp. 586-590
    • Aubert, C.1    Vos, M.H.2    Mathis, P.3    Eker, A.P.4    Brettel, K.5
  • 43
    • 0037424379 scopus 로고    scopus 로고
    • 2 resistance mediated by streptococcal Dpr: demonstration of the functional involvement of the putative ferroxidase center by site-directed mutagenesis in Streptococcus suis
    • 2 resistance mediated by streptococcal Dpr: demonstration of the functional involvement of the putative ferroxidase center by site-directed mutagenesis in Streptococcus suis. J. Biol. Chem. 278 (2003) 7996-8005
    • (2003) J. Biol. Chem. , vol.278 , pp. 7996-8005
    • Pullianien, A.T.1    Haataja, S.2    Kähkönen, S.3    Finne, J.4
  • 45
    • 15844374760 scopus 로고    scopus 로고
    • The Dps-like protein Fri of Listeria monocytogenes promotes stress tolerance and intracellular multiplication in macrophages-like cells
    • Olsen K.N., Larsen M.H., Gahan C.G., Kallipolitis B., Wolf X.A., Rea R., Hill C., and Ingmer H. The Dps-like protein Fri of Listeria monocytogenes promotes stress tolerance and intracellular multiplication in macrophages-like cells. Microbiology 151 (2005) 925-933
    • (2005) Microbiology , vol.151 , pp. 925-933
    • Olsen, K.N.1    Larsen, M.H.2    Gahan, C.G.3    Kallipolitis, B.4    Wolf, X.A.5    Rea, R.6    Hill, C.7    Ingmer, H.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.