메뉴 건너뛰기




Volumn 65, Issue 4, 2012, Pages 375-383

The positive effect of exogenous hemin on a resistance of strict anaerobic archaeon Methanobrevibacter arboriphilus to oxidative stresses

Author keywords

[No Author keywords available]

Indexed keywords

APOENZYME; CATALASE; HEME; HEMIN; HYDROGEN PEROXIDE; OXYGEN; PUROMYCIN;

EID: 84865983937     PISSN: 03438651     EISSN: 14320991     Source Type: Journal    
DOI: 10.1007/s00284-012-0168-6     Document Type: Article
Times cited : (9)

References (44)
  • 1
    • 0031685510 scopus 로고    scopus 로고
    • Biochemistry of methanogenesis: A tribute to Marjory Stephenson
    • Thauer RK (1998) Biochemistry of methanogenesis: a tribute to Marjory Stephenson. Microbiology 144:2377-2406
    • (1998) Microbiology , vol.144 , pp. 2377-2406
    • Thauer, R.K.1
  • 2
    • 36148942886 scopus 로고    scopus 로고
    • Aerotolerance of strictly anaerobic microorganisms and factors of defense against oxidative stress: A review
    • Brioukhanov AL, Netrusov AI (2007) Aerotolerance of strictly anaerobic microorganisms and factors of defense against oxidative stress: a review. Appl Biochem Microbiol 43:567-582
    • (2007) Appl Biochem Microbiol , vol.43 , pp. 567-582
    • Brioukhanov, A.L.1    Netrusov, A.I.2
  • 3
    • 0002806157 scopus 로고
    • Diversity and taxonomy of methanogens
    • Ferry JG (ed) Chapman & Hall, New York
    • Boone DR, Whitman WB, Rouviere P (1993) Diversity and taxonomy of methanogens. In: Ferry JG (ed) Methanogenesis. Chapman & Hall, New York, pp 35-80
    • (1993) Methanogenesis , pp. 35-80
    • Boone, D.R.1    Whitman, W.B.2    Rouviere, P.3
  • 4
    • 0029967858 scopus 로고    scopus 로고
    • Pathways of energy conservation in methanogenic archaea
    • Deppenmeier U, Muller V, Gottschalk G (1996) Pathways of energy conservation in methanogenic archaea. Arch Microbiol 165:149-163
    • (1996) Arch Microbiol , vol.165 , pp. 149-163
    • Deppenmeier, U.1    Muller, V.2    Gottschalk, G.3
  • 5
    • 0022978345 scopus 로고
    • Further studies on the distribution of cytochromes in methanogenic bacteria
    • Jussofie A, Gottschalk G (1986) Further studies on the distribution of cytochromes in methanogenic bacteria. FEMS Microbiol Lett 37:15-18
    • (1986) FEMS Microbiol Lett , vol.37 , pp. 15-18
    • Jussofie, A.1    Gottschalk, G.2
  • 6
    • 0032925305 scopus 로고    scopus 로고
    • Purification, characterization, and primary structure of a monofunctional catalase from Methanosarcina barkeri
    • Shima S, Netrusov A, Sordel M, Wicke M, Hartmann GC, Thauer RK (1999) Purification, characterization, and primary structure of a monofunctional catalase from Methanosarcina barkeri. Arch Microbiol 171:317-323
    • (1999) Arch Microbiol , vol.171 , pp. 317-323
    • Shima, S.1    Netrusov, A.2    Sordel, M.3    Wicke, M.4    Hartmann, G.C.5    Thauer, R.K.6
  • 7
    • 0028726343 scopus 로고
    • Biosynthesis of coenzyme F430, a nickel porphinoid involved in methanogenesis
    • Thauer RK, Bonacker LG (1994) Biosynthesis of coenzyme F430, a nickel porphinoid involved in methanogenesis. Ciba Found Symp 180:210-227
    • (1994) Ciba Found Symp , vol.180 , pp. 210-227
    • Thauer, R.K.1    Bonacker, L.G.2
  • 8
    • 0029782668 scopus 로고    scopus 로고
    • Physiological ecology of Methanobrevibacter cuticularis sp. nov. and Methanobrevibacter curvatus sp. nov., isolated from the hindgut of the termite Reticulitermes flavipes
    • Leadbetter JR, Breznak JA (1996) Physiological ecology of Methanobrevibacter cuticularis sp. nov. and Methanobrevibacter curvatus sp. nov., isolated from the hindgut of the termite Reticulitermes flavipes. Appl Environ Microbiol 62:3620-3631
    • (1996) Appl Environ Microbiol , vol.62 , pp. 3620-3631
    • Leadbetter, J.R.1    Breznak, J.A.2
  • 9
    • 0027380120 scopus 로고
    • Characterization of methanobrevibacter arboriphilus sa isolated from a paddy field soil and dna-dna hybridization among M. Arboriphilus strains
    • Asakawa S, Morii H, Akagawa-Matsushita M, Koga Y, Hayano K (1993) Characterization of Methanobrevibacter arboriphilus SA isolated from a paddy field soil and DNA-DNA hybridization among M. arboriphilus strains. Int J Syst Bacteriol 43:683-686
    • (1993) Int J Syst Bacteriol , vol.43 , pp. 683-686
    • Asakawa, S.1    Morii, H.2    Akagawa-Matsushita, M.3    Koga, Y.4    Hayano, K.5
  • 12
    • 84986394216 scopus 로고
    • Oxygen sensitivity of methanogenic bacteria
    • Kiener A, Leisinger T (1983) Oxygen sensitivity of methanogenic bacteria. Syst Appl Microbiol 4:305-312
    • (1983) Syst Appl Microbiol , vol.4 , pp. 305-312
    • Kiener, A.1    Leisinger, T.2
  • 13
    • 5444274434 scopus 로고    scopus 로고
    • F420H2 oxidase (FprA) from Methanobrevibacter arboriphilus, a coenzyme F420-dependent enzyme involved in O2 detoxification
    • Seedorf H, Dreisbach A, Hedderich R, Shima S, Thauer RK (2004) F420H2 oxidase (FprA) from Methanobrevibacter arboriphilus, a coenzyme F420-dependent enzyme involved in O2 detoxification. Arch Microbiol 182:126-137
    • (2004) Arch Microbiol , vol.182 , pp. 126-137
    • Seedorf, H.1    Dreisbach, A.2    Hedderich, R.3    Shima, S.4    Thauer, R.K.5
  • 14
    • 39149089337 scopus 로고    scopus 로고
    • Evaluation of methanogenic strains and their ability to endure aeration and water stress
    • Liu CT, Miyaki T, Aono T, Oyaizu H (2008) Evaluation of methanogenic strains and their ability to endure aeration and water stress. Curr Microbiol 56:214-218
    • (2008) Curr Microbiol , vol.56 , pp. 214-218
    • Liu, C.T.1    Miyaki, T.2    Aono, T.3    Oyaizu, H.4
  • 15
    • 33646189614 scopus 로고    scopus 로고
    • Purification and characterization of Fe-containing superoxide dismutase from Methanobrevibacter arboriphilus strain AZ
    • Brioukhanov AL, Nesatyy VJ, Netrusov AI (2006) Purification and characterization of Fe-containing superoxide dismutase from Methanobrevibacter arboriphilus strain AZ. Biochemistry (Mosc.) 71:441-447
    • (2006) Biochemistry (Mosc.) , vol.71 , pp. 441-447
    • Brioukhanov, A.L.1    Nesatyy, V.J.2    Netrusov, A.I.3
  • 16
    • 10044234054 scopus 로고    scopus 로고
    • Catalase and superoxide dismutase: Distribution, properties, and physiological role in cells of strict anaerobes
    • Brioukhanov AL, Netrusov AI (2004) Catalase and superoxide dismutase: distribution, properties, and physiological role in cells of strict anaerobes. Biochemistry (Mosc.) 69:949-962
    • (2004) Biochemistry (Mosc.) , vol.69 , pp. 949-962
    • Brioukhanov, A.L.1    Netrusov, A.I.2
  • 17
    • 0021043907 scopus 로고
    • Effect of heme on Bacteroides distasonis catalase and aerotolerance
    • Gregory EM, Fanning DD (1983) Effect of heme on Bacteroides distasonis catalase and aerotolerance. J Bacteriol 156:1012-1018
    • (1983) J Bacteriol , vol.156 , pp. 1012-1018
    • Gregory, E.M.1    Fanning, D.D.2
  • 19
    • 0030613766 scopus 로고    scopus 로고
    • Regulation of Bacteroides fragilis katB mRNA by oxidative stress and carbon limitation
    • Rocha ER, Smith CJ (1997) Regulation of Bacteroides fragilis katB mRNA by oxidative stress and carbon limitation. J Bacteriol 179:7033-7039
    • (1997) J Bacteriol , vol.179 , pp. 7033-7039
    • Rocha, E.R.1    Smith, C.J.2
  • 20
    • 10044288966 scopus 로고
    • Induction of catalase in the anaerobe Bacteroides distasonis by heme
    • Gregory EM, Natalie DL (1981) Induction of catalase in the anaerobe Bacteroides distasonis by heme. Fed Proc 40:1864
    • (1981) Fed Proc , vol.40 , pp. 1864
    • Gregory, E.M.1    Natalie, D.L.2
  • 21
    • 0025831111 scopus 로고
    • Roles of porphyrins and host iron transport proteins in regulation of growth of Porphyromonas gingivalis W50
    • Bramanti TE, Holt SC (1991) Roles of porphyrins and host iron transport proteins in regulation of growth of Porphyromonas gingivalis W50. J Bacteriol 173:7330-7339
    • (1991) J Bacteriol , vol.173 , pp. 7330-7339
    • Bramanti, T.E.1    Holt, S.C.2
  • 22
    • 27644590673 scopus 로고    scopus 로고
    • Catalase and superoxide dismutase in the cells of strictly anaerobic microorganisms
    • Brioukhanov AL, Thauer RK, Netrusov AI (2002) Catalase and superoxide dismutase in the cells of strictly anaerobic microorganisms. Microbiology 71:281-285
    • (2002) Microbiology , vol.71 , pp. 281-285
    • Brioukhanov, A.L.1    Thauer, R.K.2    Netrusov, A.I.3
  • 23
    • 0035805166 scopus 로고    scopus 로고
    • The ''strict anaerobe'' Desulfovibrio gigas contains a membrane-bound oxygen-reducing respiratory chain
    • Lemos RS, Gomes CM, Santana M, LeGall J, Xavier AV, Teixeira M (2001) The ''strict anaerobe'' Desulfovibrio gigas contains a membrane-bound oxygen-reducing respiratory chain. FEBS Lett 496:40-43
    • (2001) FEBS Lett , vol.496 , pp. 40-43
    • Lemos, R.S.1    Gomes, C.M.2    Santana, M.3    Legall, J.4    Xavier, A.V.5    Teixeira, M.6
  • 24
    • 14644397208 scopus 로고    scopus 로고
    • Cytochrome bd oxidase, oxidative stress, and dioxygen tolerance of the strictly anaerobic bacterium Moorella thermoacetica
    • Das A, Silaghi-Dumitrescu R, Ljungdahl LG, Kurtz DM (2005) Cytochrome bd oxidase, oxidative stress, and dioxygen tolerance of the strictly anaerobic bacterium Moorella thermoacetica. J Bacteriol 187:2020-2029
    • (2005) J Bacteriol , vol.187 , pp. 2020-2029
    • Das, A.1    Silaghi-Dumitrescu, R.2    Ljungdahl, L.G.3    Kurtz, D.M.4
  • 25
    • 2342475768 scopus 로고    scopus 로고
    • The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough
    • Heidelberg J, Seshadri R, Haveman S et al (2004) The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough. Nat Biotechnol 22:554-559
    • (2004) Nat Biotechnol , vol.22 , pp. 554-559
    • Heidelberg, J.1    Seshadri, R.2    Haveman, S.3
  • 26
    • 56449103177 scopus 로고    scopus 로고
    • The haem-copper oxygen reductase of Desulfovibrio vulgaris contains a dihaem cytochrome c in subunit II
    • Lobo S, Almeida C, Carita J, Teixeira M, Saraiva L (2008) The haem-copper oxygen reductase of Desulfovibrio vulgaris contains a dihaem cytochrome c in subunit II. Biochim Biophys Acta 1777:1528-1534
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 1528-1534
    • Lobo, S.1    Almeida, C.2    Carita, J.3    Teixeira, M.4    Saraiva, L.5
  • 27
    • 5444249703 scopus 로고    scopus 로고
    • Characterization of a heme oxygenase of Clostridium tetani and its possible role in oxygen tolerance
    • Bruggemann H, Bauer R, Raffestin S, Gottschalk G (2004) Characterization of a heme oxygenase of Clostridium tetani and its possible role in oxygen tolerance. Arch Microbiol 182: 259-263
    • (2004) Arch Microbiol , vol.182 , pp. 259-263
    • Bruggemann, H.1    Bauer, R.2    Raffestin, S.3    Gottschalk, G.4
  • 28
    • 0015416039 scopus 로고
    • Enthalpy of decomposition of hydrogen peroxide by catalase at 25 °c (with molar extinction coefficients of H2O2 solutions in the UV)
    • Nelson DP, Kiesow LA (1972) Enthalpy of decomposition of hydrogen peroxide by catalase at 25 °C (with molar extinction coefficients of H2O2 solutions in the UV). Anal Biochem 49:474-478
    • (1972) Anal Biochem , vol.49 , pp. 474-478
    • Nelson, D.P.1    Kiesow, L.A.2
  • 29
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 30
    • 0026318447 scopus 로고
    • Hemin: A possible physiological mediator of low density lipoprotein oxidation and endothelial injury
    • Balla G, Jacob HS, Eaton JW, Belcher JD, Vercellotti GM (1991) Hemin: a possible physiological mediator of low density lipoprotein oxidation and endothelial injury. Arterioscler Thromb 11:1700-1711
    • (1991) Arterioscler Thromb , vol.11 , pp. 1700-1711
    • Balla, G.1    Jacob, H.S.2    Eaton, J.W.3    Belcher, J.D.4    Vercellotti, G.M.5
  • 31
    • 0021288059 scopus 로고
    • Paraquat: Model for oxidant-initiated toxicity
    • Bus JS, Gibson JE (1984) Paraquat: model for oxidant-initiated toxicity. Environ Health Perspect 55:37-46
    • (1984) Environ Health Perspect , vol.55 , pp. 37-46
    • Bus, J.S.1    Gibson, J.E.2
  • 32
    • 0031980272 scopus 로고    scopus 로고
    • Oxygen-dependent regulation of the expression of the catalase gene katA of Lactobacillus sakei LTH677
    • Hertel C, Schmidt G, Fischer M, Oellers K, Hammes WP (1998) Oxygen-dependent regulation of the expression of the catalase gene katA of Lactobacillus sakei LTH677. Appl Environ Microbiol 64:1359-1365
    • (1998) Appl Environ Microbiol , vol.64 , pp. 1359-1365
    • Hertel, C.1    Schmidt, G.2    Fischer, M.3    Oellers, K.4    Hammes, W.P.5
  • 33
    • 0029009966 scopus 로고
    • Ferrochelatase activity and protoporphyrin IX utilization in Haemophilus influenzae
    • Loeb MR (1995) Ferrochelatase activity and protoporphyrin IX utilization in Haemophilus influenzae. J Bacteriol 177:3613-3615
    • (1995) J Bacteriol , vol.177 , pp. 3613-3615
    • Loeb, M.R.1
  • 34
    • 0029019571 scopus 로고
    • Biochemical and genetic analyses of a catalase from the anaerobic bacterium Bacteroides fragilis
    • Rocha ER, Smith CJ (1995) Biochemical and genetic analyses of a catalase from the anaerobic bacterium Bacteroides fragilis. J Bacteriol 177:3111-3119
    • (1995) J Bacteriol , vol.177 , pp. 3111-3119
    • Rocha, E.R.1    Smith, C.J.2
  • 35
    • 0029039266 scopus 로고
    • The termite microflora as an oxygen sink: Microelectrode determination of oxygen and pH gradients in guts of lower and higher termites
    • Brune A, Emerson D, Breznak JA (1995) The termite microflora as an oxygen sink: microelectrode determination of oxygen and pH gradients in guts of lower and higher termites. Appl Environ Microbiol 61:2681-2687
    • (1995) Appl Environ Microbiol , vol.61 , pp. 2681-2687
    • Brune, A.1    Emerson, D.2    Breznak, J.A.3
  • 36
    • 0035175194 scopus 로고    scopus 로고
    • The NADH oxidase from Pyrococcus furiosus. Implications for the protection of anaerobic hyperthermophiles against oxidative stress
    • Ward DE, Donnelly CJ, Mullendore ME, van der Oost J, de Vos WM, Crane EJ (2001) The NADH oxidase from Pyrococcus furiosus. Implications for the protection of anaerobic hyperthermophiles against oxidative stress. Eur J Biochem 268:5816-5823
    • (2001) Eur J Biochem , vol.268 , pp. 5816-5823
    • Ward, D.E.1    Donnelly, C.J.2    Mullendore, M.E.3    Van Der Oost, J.4    De Vos, W.M.5    Crane, E.J.6
  • 37
    • 77953024133 scopus 로고    scopus 로고
    • Oxidative stress protection and the repair response to hydrogen peroxide in the hyperthermophilic archaeon Pyrococcus furiosus and in related species
    • Strand KR, Sun C, Li T, Jenney FE, Schut GJ, Adams MW (2010) Oxidative stress protection and the repair response to hydrogen peroxide in the hyperthermophilic archaeon Pyrococcus furiosus and in related species. Arch Microbiol 192:447-459
    • (2010) Arch Microbiol , vol.192 , pp. 447-459
    • Strand, K.R.1    Sun, C.2    Li, T.3    Jenney, F.E.4    Schut, G.J.5    Adams, M.W.6
  • 38
    • 13644264825 scopus 로고    scopus 로고
    • Oxidative stress response in an anaerobic hyperthermophilic archaeon: Presence of a functional peroxiredoxin in Pyrococcus horikoshii
    • Kawakami R, Sakuraba H, Kamohara S, Goda S, Kawarabayasi Y, Ohshima T (2004) Oxidative stress response in an anaerobic hyperthermophilic archaeon: presence of a functional peroxiredoxin in Pyrococcus horikoshii. J Biochem 136:541-547
    • (2004) J Biochem , vol.136 , pp. 541-547
    • Kawakami, R.1    Sakuraba, H.2    Kamohara, S.3    Goda, S.4    Kawarabayasi, Y.5    Ohshima, T.6
  • 39
    • 0017615340 scopus 로고
    • Physiology of a Methanobacterium strain AZ
    • Zehnder AJB, Wuhrmann K (1977) Physiology of a Methanobacterium strain AZ. Arch Microbiol 111:199-205
    • (1977) Arch Microbiol , vol.111 , pp. 199-205
    • Ajb, Z.1    Wuhrmann, K.2
  • 40
    • 0016604562 scopus 로고
    • Methanobacterium arboriphilicum sp. nov. An obligate anaerobe isolated from wetwood of living trees
    • Zeikus JG, Henning DL (1975) Methanobacterium arboriphilicum sp. nov. An obligate anaerobe isolated from wetwood of living trees. Antonie Leeuwenhoek 41:543-552
    • (1975) Antonie Leeuwenhoek , vol.41 , pp. 543-552
    • Zeikus, J.G.1    Henning, D.L.2
  • 41
    • 0020791903 scopus 로고
    • Bactobilin: Blue bile pigment isolated from Clostridium tetanomorphum
    • Brumm PJ, Fried J, Friedmann HC (1983) Bactobilin: blue bile pigment isolated from Clostridium tetanomorphum. Proc Natl Acad Sci USA 80:3943-3947
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 3943-3947
    • Brumm, P.J.1    Fried, J.2    Friedmann, H.C.3
  • 42
    • 0031958936 scopus 로고    scopus 로고
    • Methanobrevibacter filiformis sp. nov., a filamentous methanogen from termite hindguts
    • Leadbetter JR, Crosby LD, Breznak JA (1998) Methanobrevibacter filiformis sp. nov., a filamentous methanogen from termite hindguts. Arch Microbiol 169:287-292
    • (1998) Arch Microbiol , vol.169 , pp. 287-292
    • Leadbetter, J.R.1    Crosby, L.D.2    Breznak, J.A.3
  • 43
    • 0027507586 scopus 로고
    • Hemin uptake in Porphyromonas gingivalis: Omp26 is a hemin-binding surface protein
    • Bramanti TE, Holt SC (1993) Hemin uptake in Porphyromonas gingivalis: Omp26 is a hemin-binding surface protein. J Bacteriol 175:7413-7420
    • (1993) J Bacteriol , vol.175 , pp. 7413-7420
    • Bramanti, T.E.1    Holt, S.C.2
  • 44
    • 0029242158 scopus 로고
    • Regulation of hemin and iron transport in Porphyromonas gingivalis
    • Genco CA (1995) Regulation of hemin and iron transport in Porphyromonas gingivalis. Adv Dent Res 9:41-47
    • (1995) Adv Dent Res , vol.9 , pp. 41-47
    • Genco, C.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.