메뉴 건너뛰기




Volumn 17, Issue 6, 2011, Pages 501-505

Identification and analysis of the Shewanella oneidensis major oxygen-independent coproporphyrinogen III oxidase gene

Author keywords

Anaerobic respiration; C type cytochromes; HemN; Shewanella oneidensis

Indexed keywords

COPROPORPHYRINOGEN OXIDASE; CYTOCHROME C;

EID: 84655167649     PISSN: 10759964     EISSN: 10958274     Source Type: Journal    
DOI: 10.1016/j.anaerobe.2011.06.008     Document Type: Article
Times cited : (3)

References (32)
  • 1
    • 0024219883 scopus 로고
    • Bacterial manganese reduction and growth with manganese oxide as the sole electron acceptor
    • Myers C., Nealson K. Bacterial manganese reduction and growth with manganese oxide as the sole electron acceptor. Science 1988, 240:1319-1321.
    • (1988) Science , vol.240 , pp. 1319-1321
    • Myers, C.1    Nealson, K.2
  • 3
    • 0036842611 scopus 로고    scopus 로고
    • Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis
    • Heidelberg J., Paulsen I., Nealson K., Gaidos E., Nelson W., Read T., et al. Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis. Nat Biotechnol 2002, 20:1118-1123.
    • (2002) Nat Biotechnol , vol.20 , pp. 1118-1123
    • Heidelberg, J.1    Paulsen, I.2    Nealson, K.3    Gaidos, E.4    Nelson, W.5    Read, T.6
  • 5
    • 0028132223 scopus 로고
    • Iron and Manganese in anaerobic respiration: environmental significance, physiology, and regulation
    • Nealson K., Saffarini D. Iron and Manganese in anaerobic respiration: environmental significance, physiology, and regulation. Ann Rev Microbiol 1994, 48:311-343.
    • (1994) Ann Rev Microbiol , vol.48 , pp. 311-343
    • Nealson, K.1    Saffarini, D.2
  • 6
    • 18044401289 scopus 로고    scopus 로고
    • Identification of a small tetraheme cytochrome c and a flavocytochrome c as two of the principal soluble cytochromes c in Shewanella oneidensis strain MR1
    • Tsapin A.I., Vandenberghe I., Nealson K.H., Scott J.H., Meyer T.E., Cusanovich M.A., et al. Identification of a small tetraheme cytochrome c and a flavocytochrome c as two of the principal soluble cytochromes c in Shewanella oneidensis strain MR1. Appl Environ Microbiol 2001, 67:3236-3244.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 3236-3244
    • Tsapin, A.I.1    Vandenberghe, I.2    Nealson, K.H.3    Scott, J.H.4    Meyer, T.E.5    Cusanovich, M.A.6
  • 7
    • 0030903069 scopus 로고    scopus 로고
    • Outer membrane cytochromes of Shewanella putrefaciens MR-1: spectral analysis, and purification of the 83-kDa c-type cytochrome
    • Myers C., Myers J. Outer membrane cytochromes of Shewanella putrefaciens MR-1: spectral analysis, and purification of the 83-kDa c-type cytochrome. Biochim Biophys Acta 1997, 1326:307-318.
    • (1997) Biochim Biophys Acta , vol.1326 , pp. 307-318
    • Myers, C.1    Myers, J.2
  • 8
    • 0042378909 scopus 로고    scopus 로고
    • Cell surface exposure of the outer membrane cytochromes of Shewanella oneidensis MR-1
    • Myers C.R., Myers J.M. Cell surface exposure of the outer membrane cytochromes of Shewanella oneidensis MR-1. Lett Appl Microbiol 2003, 37:254-258.
    • (2003) Lett Appl Microbiol , vol.37 , pp. 254-258
    • Myers, C.R.1    Myers, J.M.2
  • 9
    • 0038817925 scopus 로고    scopus 로고
    • Overlapping role of the outer membrane cytochromes of Shewanella oneidensis MR-1 in the reduction of manganese(IV) oxide
    • Myers J., Myers C. Overlapping role of the outer membrane cytochromes of Shewanella oneidensis MR-1 in the reduction of manganese(IV) oxide. Lett Appl Microbiol 2003, 37:21-25.
    • (2003) Lett Appl Microbiol , vol.37 , pp. 21-25
    • Myers, J.1    Myers, C.2
  • 10
    • 0035131413 scopus 로고    scopus 로고
    • MtrC, an outer membrane decaheme c cytochrome required for metal reduction in Shewanella putrefaciens MR-1
    • Beliaev A., Saffarini D., McLaughlin J., Hunnicut D. MtrC, an outer membrane decaheme c cytochrome required for metal reduction in Shewanella putrefaciens MR-1. Mol Microbiol 2001, 39:722-730.
    • (2001) Mol Microbiol , vol.39 , pp. 722-730
    • Beliaev, A.1    Saffarini, D.2    McLaughlin, J.3    Hunnicut, D.4
  • 11
    • 23744508420 scopus 로고    scopus 로고
    • Identification of genes involved in cytochrome c biogenesis in Shewanella oneidensis, using a modified mariner transposon
    • Bouhenni R., Gehrke A., Saffarini D. Identification of genes involved in cytochrome c biogenesis in Shewanella oneidensis, using a modified mariner transposon. Appl Environ Microbiol 2005, 71:4935-4937.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 4935-4937
    • Bouhenni, R.1    Gehrke, A.2    Saffarini, D.3
  • 12
    • 33645224039 scopus 로고    scopus 로고
    • Extracellular respiration of dimethyl sulfoxide by Shewanella oneidensis strain MR-1
    • Gralnick J.A., Vali H., Lies D.P., Newman D.K. Extracellular respiration of dimethyl sulfoxide by Shewanella oneidensis strain MR-1. Proc Natl Acad Sci U S A 2006, 103:4669-4674.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4669-4674
    • Gralnick, J.A.1    Vali, H.2    Lies, D.P.3    Newman, D.K.4
  • 14
    • 0036670802 scopus 로고    scopus 로고
    • Terminal steps in haem biosynthesis
    • Dailey H.A. Terminal steps in haem biosynthesis. Biochem Soc Trans 2002, 30:590-595.
    • (2002) Biochem Soc Trans , vol.30 , pp. 590-595
    • Dailey, H.A.1
  • 16
    • 0035143945 scopus 로고    scopus 로고
    • One of two hemN genes in Bradyrhizobium japonicum is functional during anaerobic growth and symbiosis
    • Fischer H., Velasco L., Delgado M., Bedmar E., Scharen S., Zingg D., et al. One of two hemN genes in Bradyrhizobium japonicum is functional during anaerobic growth and symbiosis. JBacteriol 2001, 183:1300-1311.
    • (2001) JBacteriol , vol.183 , pp. 1300-1311
    • Fischer, H.1    Velasco, L.2    Delgado, M.3    Bedmar, E.4    Scharen, S.5    Zingg, D.6
  • 17
    • 0031909199 scopus 로고    scopus 로고
    • The Alcalignes eutrophus hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase is required for heme biosynthesis during anaerobic growth
    • Lieb C., Sidiqui R., Hippler B., Jahn D., Freidrich B. The Alcalignes eutrophus hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase is required for heme biosynthesis during anaerobic growth. Arch Microbiol 1998, 169:52-60.
    • (1998) Arch Microbiol , vol.169 , pp. 52-60
    • Lieb, C.1    Sidiqui, R.2    Hippler, B.3    Jahn, D.4    Freidrich, B.5
  • 18
    • 0029009423 scopus 로고
    • Cloning and characterization of the E.coli hemN gene encoding the oxygen-independent coproporphyriongen III oxidase
    • Troup B., Hungerer C., Jahn D. Cloning and characterization of the E.coli hemN gene encoding the oxygen-independent coproporphyriongen III oxidase. JBacteriol 1995, 177:3326-3331.
    • (1995) JBacteriol , vol.177 , pp. 3326-3331
    • Troup, B.1    Hungerer, C.2    Jahn, D.3
  • 19
    • 0028107485 scopus 로고
    • Isolation of hemF operon containing the gene for the E.coli aerobic coproporphyrinogen III oxidase by invivo complementation of a yeast HEM13 mutant
    • Troup B., Jahn M., Hungerer C., Jahn D. Isolation of hemF operon containing the gene for the E.coli aerobic coproporphyrinogen III oxidase by invivo complementation of a yeast HEM13 mutant. JBacteriol 1994, 176:673-680.
    • (1994) JBacteriol , vol.176 , pp. 673-680
    • Troup, B.1    Jahn, M.2    Hungerer, C.3    Jahn, D.4
  • 20
    • 0028304529 scopus 로고
    • Cloning, DNA sequence, and complementation analysis of Salmonella typhimurium hemN gene encoding a putative oxygen-independent coproporphyrinogen III oxidase
    • Xu K., Elliott T. Cloning, DNA sequence, and complementation analysis of Salmonella typhimurium hemN gene encoding a putative oxygen-independent coproporphyrinogen III oxidase. JBacteriol 1994, 176:3196-3203.
    • (1994) JBacteriol , vol.176 , pp. 3196-3203
    • Xu, K.1    Elliott, T.2
  • 21
    • 0031754775 scopus 로고    scopus 로고
    • Shewanella putrefaciens mtrB encodes an outer membrane protein required for Fe(III) and Mn(IV) reduction
    • Beliaev A., Saffarini D. Shewanella putrefaciens mtrB encodes an outer membrane protein required for Fe(III) and Mn(IV) reduction. JBacteriol 1998, 180:6292-6297.
    • (1998) JBacteriol , vol.180 , pp. 6292-6297
    • Beliaev, A.1    Saffarini, D.2
  • 22
    • 0015040637 scopus 로고
    • Spectrophotometric determination of serum iron at the submicron level with new reagent (ferrozine)
    • Carter P. Spectrophotometric determination of serum iron at the submicron level with new reagent (ferrozine). Anal Biochem 1971, 40:450-458.
    • (1971) Anal Biochem , vol.40 , pp. 450-458
    • Carter, P.1
  • 23
    • 0030942268 scopus 로고    scopus 로고
    • Construction and use of a versatile set of broad-host-range cloning and expression vectors based on the RK2 replicon
    • Blatny J.M., Brautaset T., Winther-Larsen H.C., Haugan K., Valla S. Construction and use of a versatile set of broad-host-range cloning and expression vectors based on the RK2 replicon. Appl Environ Microbiol 1997, 63:370-379.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 370-379
    • Blatny, J.M.1    Brautaset, T.2    Winther-Larsen, H.C.3    Haugan, K.4    Valla, S.5
  • 24
    • 0038308456 scopus 로고    scopus 로고
    • Neutralization of toxic heme by Plasmodium falciparum histidine-rich protein 2
    • Huy N., Serada S., Trang D., Takano R., Kondo Y., Kanaori K., et al. Neutralization of toxic heme by Plasmodium falciparum histidine-rich protein 2. JBiochem 2003, 133:693-698.
    • (2003) JBiochem , vol.133 , pp. 693-698
    • Huy, N.1    Serada, S.2    Trang, D.3    Takano, R.4    Kondo, Y.5    Kanaori, K.6
  • 25
    • 0017170673 scopus 로고
    • An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dedecyl sulfate polyacrylamide gels
    • Thomas P.E., Ryan D., Levin W. An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dedecyl sulfate polyacrylamide gels. Anal Biochem 1976, 168-176.
    • (1976) Anal Biochem , pp. 168-176
    • Thomas, P.E.1    Ryan, D.2    Levin, W.3
  • 26
    • 0037990786 scopus 로고    scopus 로고
    • Biogenesis of respiratory cytochromes in bacteria
    • Thony-Meyer L. Biogenesis of respiratory cytochromes in bacteria. Microbiol Mol Biol Rev 1997, 61:337-376.
    • (1997) Microbiol Mol Biol Rev , vol.61 , pp. 337-376
    • Thony-Meyer, L.1
  • 27
    • 15144342710 scopus 로고    scopus 로고
    • Regulation of Pseudomonas aeruginosa hemF and hemN by dual action of the redox response regulator ANR and DNR
    • Rompf A., Hungerer C., Hoffmann T., Lindenmeyer M., Römling U., Gross U., et al. Regulation of Pseudomonas aeruginosa hemF and hemN by dual action of the redox response regulator ANR and DNR. Mol Microbiol 1998, 29:985-997.
    • (1998) Mol Microbiol , vol.29 , pp. 985-997
    • Rompf, A.1    Hungerer, C.2    Hoffmann, T.3    Lindenmeyer, M.4    Römling, U.5    Gross, U.6
  • 28
    • 0020611838 scopus 로고
    • Anaerobic and aerobic coproporphyrinogen III oxidases in of Rhodopseudomonas sphaeroides. Mechanism and stereochemistry of vinyl group formation
    • Seehra J., Jordan P., Akhtar M. Anaerobic and aerobic coproporphyrinogen III oxidases in of Rhodopseudomonas sphaeroides. Mechanism and stereochemistry of vinyl group formation. Biochem J 1983, 209:709-718.
    • (1983) Biochem J , vol.209 , pp. 709-718
    • Seehra, J.1    Jordan, P.2    Akhtar, M.3
  • 29
    • 0027205487 scopus 로고
    • An Oxygen-dependent coproporphyrinogen oxidase encoded by the hemF gene of Salmonella typhimurium
    • Xu D., Elliot T. An Oxygen-dependent coproporphyrinogen oxidase encoded by the hemF gene of Salmonella typhimurium. JBacteriol 1993, 175:4990-4999.
    • (1993) JBacteriol , vol.175 , pp. 4990-4999
    • Xu, D.1    Elliot, T.2
  • 30
    • 0026688997 scopus 로고
    • The genes required for heme synthesis in Salmonella typhimurium include those encoding alternative functions for aerobic and anaerobic coproporphyrinogen oxidation
    • Xu K., Delling J., Elliott T. The genes required for heme synthesis in Salmonella typhimurium include those encoding alternative functions for aerobic and anaerobic coproporphyrinogen oxidation. JBacteriol 1992, 174:3953-3963.
    • (1992) JBacteriol , vol.174 , pp. 3953-3963
    • Xu, K.1    Delling, J.2    Elliott, T.3
  • 31
    • 0037072870 scopus 로고    scopus 로고
    • Oxygen-independent coproporphyrinogen III oxidase hemN from Escherichia coli
    • Layer G., Verfurth K., Mahlitz E., Jahn D. Oxygen-independent coproporphyrinogen III oxidase hemN from Escherichia coli. JBiol Chem 2002, 277:34136-34142.
    • (2002) JBiol Chem , vol.277 , pp. 34136-34142
    • Layer, G.1    Verfurth, K.2    Mahlitz, E.3    Jahn, D.4
  • 32
    • 0021027842 scopus 로고
    • Abroad host range mobilization system for invivo genetic engineering: transposon mutagenesis in Gram negative bacteria
    • Simon R., Priefer U., Puhler A. Abroad host range mobilization system for invivo genetic engineering: transposon mutagenesis in Gram negative bacteria. Biotechnology 1983, 1:784-791.
    • (1983) Biotechnology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.