메뉴 건너뛰기




Volumn 110, Issue 15, 2013, Pages 5945-5950

Responses of Mn2+ speciation in Deinococcus radiodurans and Escherichia coli to γ-radiation by advanced paramagnetic resonance methods

Author keywords

Cellular radiation resistance; Desiccation; ENDOR; ESEEM; UVC

Indexed keywords

MANGANESE; SUPEROXIDE DISMUTASE; ANTIOXIDANT; BACTERIAL PROTEIN; LIGAND; REACTIVE OXYGEN METABOLITE; SODA PROTEIN, BACTERIA;

EID: 84876040028     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1303376110     Document Type: Article
Times cited : (70)

References (35)
  • 1
    • 8344278843 scopus 로고    scopus 로고
    • Accumulation of Mn (II) in Deinococcus radiodurans facilitates gamma-radiation resistance
    • Daly MJ, et al. (2004) Accumulation of Mn (II) in Deinococcus radiodurans facilitates gamma-radiation resistance. Science 306(5698):1025-1028.
    • (2004) Science , vol.306 , Issue.5698 , pp. 1025-1028
    • Daly, M.J.1
  • 2
    • 84855352363 scopus 로고    scopus 로고
    • Death by protein damage in irradiated cells
    • Daly MJ (2012) Death by protein damage in irradiated cells. DNA Repair (Amst) 11(1):12-21.
    • (2012) DNA Repair (Amst) , vol.11 , Issue.1 , pp. 12-21
    • Daly, M.J.1
  • 3
    • 84859976622 scopus 로고    scopus 로고
    • Battles with iron: Manganese in oxidative stress protection
    • Aguirre JD, Culotta VC (2012) Battles with iron: Manganese in oxidative stress protection. J Biol Chem 287(17):13541-13548.
    • (2012) J Biol Chem , vol.287 , Issue.17 , pp. 13541-13548
    • Aguirre, J.D.1    Culotta, V.C.2
  • 4
    • 65549107862 scopus 로고    scopus 로고
    • Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli
    • Anjem A, Varghese S, Imlay JA (2009) Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli. Mol Microbiol 72(4):844-858.
    • (2009) Mol Microbiol , vol.72 , Issue.4 , pp. 844-858
    • Anjem, A.1    Varghese, S.2    Imlay, J.A.3
  • 5
    • 0036612888 scopus 로고    scopus 로고
    • Manganese supplementation relieves the phenotypic deficits seen in superoxide-dismutase-null Escherichia coli
    • Al-Maghrebi M, Fridovich I, Benov L (2002) Manganese supplementation relieves the phenotypic deficits seen in superoxide-dismutase-null Escherichia coli. Arch Biochem Biophys 402(1):104-109.
    • (2002) Arch Biochem Biophys , vol.402 , Issue.1 , pp. 104-109
    • Al-Maghrebi, M.1    Fridovich, I.2    Benov, L.3
  • 6
    • 79952799384 scopus 로고    scopus 로고
    • A major role for nonenzymatic antioxidant processes in the radioresistance of Halobacterium salinarum
    • Robinson CK, et al. (2011) A major role for nonenzymatic antioxidant processes in the radioresistance of Halobacterium salinarum. J Bacteriol 193(7):1653-1662.
    • (2011) J Bacteriol , vol.193 , Issue.7 , pp. 1653-1662
    • Robinson, C.K.1
  • 7
    • 60749095652 scopus 로고    scopus 로고
    • A new perspective on radiation resistance based on Deinococcus radiodurans
    • Daly MJ (2009) A new perspective on radiation resistance based on Deinococcus radiodurans. Nat Rev Microbiol 7(3):237-245.
    • (2009) Nat Rev Microbiol , vol.7 , Issue.3 , pp. 237-245
    • Daly, M.J.1
  • 8
    • 79952424488 scopus 로고    scopus 로고
    • Oxidative stress resistance in Deinococcus radiodurans
    • Slade D, Radman M (2011) Oxidative stress resistance in Deinococcus radiodurans. Microbiol Mol Biol Rev 75(1):133-191.
    • (2011) Microbiol Mol Biol Rev , vol.75 , Issue.1 , pp. 133-191
    • Slade, D.1    Radman, M.2
  • 9
    • 34247375191 scopus 로고    scopus 로고
    • Protein oxidation implicated as the primary determinant of bacterial radioresistance
    • Daly MJ, et al. (2007) Protein oxidation implicated as the primary determinant of bacterial radioresistance. PLoS Biol 5(4):e92.
    • (2007) PLoS Biol , vol.5 , Issue.4
    • Daly, M.J.1
  • 10
    • 77956269639 scopus 로고    scopus 로고
    • Protein damage and death by radiation in Escherichia coli and Deinococcus radiodurans
    • Krisko A, Radman M (2010) Protein damage and death by radiation in Escherichia coli and Deinococcus radiodurans. Proc Natl Acad Sci USA 107(32):14373-14377.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.32 , pp. 14373-14377
    • Krisko, A.1    Radman, M.2
  • 11
    • 84876069749 scopus 로고    scopus 로고
    • Manganese complexes: Diverse metabolic routes to oxidative stress resistance in prokaryotes and yeast
    • 10.1089/ars.2012.5093
    • Culotta VC, Daly MJ (2012) Manganese complexes: Diverse metabolic routes to oxidative stress resistance in prokaryotes and yeast. Antioxid Redox Signal, 10.1089/ars.2012.5093.
    • (2012) Antioxid Redox Signal
    • Culotta, V.C.1    Daly, M.J.2
  • 12
    • 84860798289 scopus 로고    scopus 로고
    • Biologically relevant mechanism for catalytic superoxide removal by simple manganese compounds
    • Barnese K, Gralla EB, Valentine JS, Cabelli DE (2012) Biologically relevant mechanism for catalytic superoxide removal by simple manganese compounds. Proc Natl Acad Sci USA 109(18):6892-6897.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.18 , pp. 6892-6897
    • Barnese, K.1    Gralla, E.B.2    Valentine, J.S.3    Cabelli, D.E.4
  • 13
    • 77958575130 scopus 로고    scopus 로고
    • Small-molecule antioxidant proteome-shields in Deinococcus radiodurans
    • Daly MJ, et al. (2010) Small-molecule antioxidant proteome-shields in Deinococcus radiodurans. PLoS ONE 5(9):e12570.
    • (2010) PLoS ONE , vol.5 , Issue.9
    • Daly, M.J.1
  • 14
    • 84871364810 scopus 로고    scopus 로고
    • 2+ and compatible solutes in the radiation resistance of thermophilic bacteria and archaea
    • 2+ and compatible solutes in the radiation resistance of thermophilic bacteria and archaea. Archaea 2012:845756.
    • (2012) Archaea , vol.2012 , pp. 845756
    • Webb, K.M.1    DiRuggiero, J.2
  • 15
    • 84872007212 scopus 로고    scopus 로고
    • 2+-Peptide complex from Deinococcus
    • 2+-Peptide complex from Deinococcus. Cell Host Microbe 12(1):117-124.
    • (2012) Cell Host Microbe , vol.12 , Issue.1 , pp. 117-124
    • Gaidamakova, E.K.1
  • 16
    • 84874064256 scopus 로고    scopus 로고
    • In situ determination of manganese (II) speciation in Deinococcus radiodurans by high magnetic-field EPR: Detection of high levels of Mn (II) bound to proteins
    • Tabares LC, Un S (2013) In situ determination of manganese (II) speciation in Deinococcus radiodurans by high magnetic-field EPR: Detection of high levels of Mn (II) bound to proteins. J Biol Chem 288(7):5050-5055.
    • (2013) J Biol Chem , vol.288 , Issue.7 , pp. 5050-5055
    • Tabares, L.C.1    Un, S.2
  • 17
    • 77957262775 scopus 로고    scopus 로고
    • 2+ speciation and oxidative stress resistance in yeast cells with ENDOR spectroscopy
    • 2+ speciation and oxidative stress resistance in yeast cells with ENDOR spectroscopy. Proc Natl Acad Sci USA 107(35):15335-15339.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.35 , pp. 15335-15339
    • McNaughton, R.L.1
  • 19
    • 0002447550 scopus 로고
    • EPR of Mn (II) complexes with enzymes and other proteins
    • Berliner LJ, Reuben J Plenum, New York, London
    • Reed GH, Markham GD (1984) EPR of Mn (II) complexes with enzymes and other proteins. Biological Magnetic Resonance, eds Berliner LJ, Reuben J (Plenum, New York, London), Vol 6, pp 73-142.
    • (1984) Biological Magnetic Resonance , vol.6 , pp. 73-142
    • Reed, G.H.1    Markham, G.D.2
  • 21
    • 0025837726 scopus 로고
    • Electron spin echo envelope modulation studies of lectins: Evidence for a conserved Mn (2+)-binding site
    • McCracken J, Peisach J, Bhattacharyya L, Brewer F (1991) Electron spin echo envelope modulation studies of lectins: Evidence for a conserved Mn (2+)-binding site. Biochemistry 30(18):4486-4491.
    • (1991) Biochemistry , vol.30 , Issue.18 , pp. 4486-4491
    • McCracken, J.1    Peisach, J.2    Bhattacharyya, L.3    Brewer, F.4
  • 22
    • 0038338712 scopus 로고    scopus 로고
    • 2+ binding site in single crystals of concanavalin A revealed by high-field EPR spectroscopy
    • 2+ binding site in single crystals of concanavalin A revealed by high-field EPR spectroscopy. Biochemistry 42(25):7863-7870.
    • (2003) Biochemistry , vol.42 , Issue.25 , pp. 7863-7870
    • Carmieli, R.1
  • 23
    • 0037070585 scopus 로고    scopus 로고
    • EPR study of substrate binding to the Mn (II) active site of the bacterial antibiotic resistance enzyme FosA: A better way to examine Mn (II)
    • Smoukov SK, et al. (2002) EPR study of substrate binding to the Mn (II) active site of the bacterial antibiotic resistance enzyme FosA: A better way to examine Mn (II). J Am Chem Soc 124(10):2318-2326.
    • (2002) J Am Chem Soc , vol.124 , Issue.10 , pp. 2318-2326
    • Smoukov, S.K.1
  • 24
    • 1542287644 scopus 로고    scopus 로고
    • Manganese (II) zero-field interaction in cambialistic and manganese superoxide dismutases and its relationship to the structure of the metal binding site
    • Un S, Tabares LC, Cortez N, Hiraoka BY, Yamakura F (2004) Manganese (II) zero-field interaction in cambialistic and manganese superoxide dismutases and its relationship to the structure of the metal binding site. J Am Chem Soc 126(9):2720-2726.
    • (2004) J Am Chem Soc , vol.126 , Issue.9 , pp. 2720-2726
    • Un, S.1    Tabares, L.C.2    Cortez, N.3    Hiraoka, B.Y.4    Yamakura, F.5
  • 25
    • 0037143692 scopus 로고    scopus 로고
    • Global analysis of the Deinococcus radiodurans proteome by using accurate mass tags
    • Lipton MS, et al. (2002) Global analysis of the Deinococcus radiodurans proteome by using accurate mass tags. Proc Natl Acad Sci USA 99(17):11049-11054.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.17 , pp. 11049-11054
    • Lipton, M.S.1
  • 26
    • 33846371934 scopus 로고    scopus 로고
    • 2+ complexes of ADP and ATPgS by W-band ENDOR
    • 2+ complexes of ADP and ATPgS by W-band ENDOR. Appl Magn Reson 30(3-4):461-472.
    • (2006) Appl Magn Reson , vol.30 , Issue.3-4 , pp. 461-472
    • Potapov, A.1    Goldfarb, D.2
  • 27
    • 80053335564 scopus 로고    scopus 로고
    • Probing conformational variations at the ATPase site of the RNA helicase DbpA by high-field electron-nuclear double resonance spectroscopy
    • Kaminker I, et al. (2011) Probing conformational variations at the ATPase site of the RNA helicase DbpA by high-field electron-nuclear double resonance spectroscopy. J Am Chem Soc 133(39):15514-15523.
    • (2011) J Am Chem Soc , vol.133 , Issue.39 , pp. 15514-15523
    • Kaminker, I.1
  • 29
    • 0034639915 scopus 로고    scopus 로고
    • W-band ENDOR investigation of the manganese-binding site of concanavalin A: Determination of proton hyperfine couplings and their signs
    • Manikandan P, Carmieli R, Shane T, Kalb AJ, Goldfarb D (2000) W-band ENDOR investigation of the manganese-binding site of concanavalin A: Determination of proton hyperfine couplings and their signs. J Am Chem Soc 122(14):3488-3494.
    • (2000) J Am Chem Soc , vol.122 , Issue.14 , pp. 3488-3494
    • Manikandan, P.1    Carmieli, R.2    Shane, T.3    Kalb, A.J.4    Goldfarb, D.5
  • 30
    • 78651340960 scopus 로고    scopus 로고
    • Combining steady-state and dynamic methods for determining absolute signs of hyperfine interactions: Pulsed ENDOR saturation and recovery (PESTRE)
    • Doan PE (2011) Combining steady-state and dynamic methods for determining absolute signs of hyperfine interactions: Pulsed ENDOR saturation and recovery (PESTRE). J Magn Reson 208(1):76-86.
    • (2011) J Magn Reson , vol.208 , Issue.1 , pp. 76-86
    • Doan, P.E.1
  • 32
    • 33846025128 scopus 로고    scopus 로고
    • EPR and HYSCORE investigation of the electronic structure of the model complex Mn (imidazole) 6: Exploring Mn (II) - Imidazole binding using single crystals
    • Garcia-Rubio I, Angerhofer A, Schweiger A (2007) EPR and HYSCORE investigation of the electronic structure of the model complex Mn (imidazole) 6: exploring Mn (II) - imidazole binding using single crystals. J Magn Reson 184(1):130-142.
    • (2007) J Magn Reson , vol.184 , Issue.1 , pp. 130-142
    • Garcia-Rubio, I.1    Angerhofer, A.2    Schweiger, A.3
  • 33
    • 0037028557 scopus 로고    scopus 로고
    • Structural analysis of metal ion ligation to nucleotides and nucleic acids using pulsed EPR spectroscopy
    • Hoogstraten CG, Grant CV, Horton TE, DeRose VJ, Britt RD (2002) Structural analysis of metal ion ligation to nucleotides and nucleic acids using pulsed EPR spectroscopy. J Am Chem Soc 124(5):834-842.
    • (2002) J Am Chem Soc , vol.124 , Issue.5 , pp. 834-842
    • Hoogstraten, C.G.1    Grant, C.V.2    Horton, T.E.3    DeRose, V.J.4    Britt, R.D.5
  • 34
    • 0034091606 scopus 로고    scopus 로고
    • Physiologic determinants of radiation resistance in Deinococcus radiodurans
    • Venkateswaran A, et al. (2000) Physiologic determinants of radiation resistance in Deinococcus radiodurans. Appl Environ Microbiol 66(6):2620-2626.
    • (2000) Appl Environ Microbiol , vol.66 , Issue.6 , pp. 2620-2626
    • Venkateswaran, A.1
  • 35
    • 0025268546 scopus 로고
    • Manganese (II) induces cell division and increases in superoxide dismutase and catalase activities in an aging deinococcal culture
    • Chou FI, Tan ST (1990) Manganese (II) induces cell division and increases in superoxide dismutase and catalase activities in an aging deinococcal culture. J Bacteriol 172(4):2029-2035.
    • (1990) J Bacteriol , vol.172 , Issue.4 , pp. 2029-2035
    • Chou, F.I.1    Tan, S.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.