메뉴 건너뛰기




Volumn 496, Issue , 2011, Pages 423-433

Detection and characterization of a multicopper oxidase from nitrosomonas Europaea

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BLUE COPPER OXIDASE; MULTICOPPER OXIDASE; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

EID: 79955503440     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-386489-5.00017-8     Document Type: Chapter
Times cited : (5)

References (31)
  • 2
    • 4744352703 scopus 로고    scopus 로고
    • Expression of nitrite reductase in Nitrosomonas europaea involves NsrR, a novel nitrite-sensitive transcription repressor
    • DOI 10.1111/j.1365-2958.2004.04248.x
    • H.J.E. Beaumont, S.I. Lens, W.N.M. Reijnders, H.V. Westerhoff, and R.J.M. van Spanning Expression of nitrite reductase in Nitrosomonas europaea involves NsrR, a novel nitrite-sensitive transcription repressor Mol. Microbiol. 54 2004 148 158 (Pubitemid 39315165)
    • (2004) Molecular Microbiology , vol.54 , Issue.1 , pp. 148-158
    • Beaumont, H.J.E.1    Lens, S.I.2    Reijnders, W.N.M.3    Westerhoff, H.V.4    Van Spanning, R.J.M.5
  • 3
    • 25144472032 scopus 로고    scopus 로고
    • Novel nirK cluster genes in Nitrosomonas europaea are required for NirK-dependent tolerance to nitrite
    • DOI 10.1128/JB.187.19.6849-6851.2005
    • H.J. Beaumont, S.I. Lens, H.V. Westerhoff, and R.J. van Spanning Novel nirK cluster genes in Nitrosomonas europaea are required for NirK-dependent tolerance to nitrite J. Bacteriol. 187 2005 6849 6851 (Pubitemid 41356260)
    • (2005) Journal of Bacteriology , vol.187 , Issue.19 , pp. 6849-6851
    • Beaumont, H.J.E.1    Lens, S.I.2    Westerhoff, H.V.3    Van Spanning, R.J.M.4
  • 8
    • 0029910752 scopus 로고    scopus 로고
    • Detection of laccase activity in polyacrylamide gels after electrophoresis under denaturing conditions
    • M.L.F.C. Goncalves, and W. Steiner Detection of laccase activity in polyacrylamide gels after electrophoresis under denaturing conditions Biotechnol. Tech. 10 1996 667 668 (Pubitemid 26368760)
    • (1996) Biotechnology Techniques , vol.10 , Issue.9 , pp. 667-668
    • Luisa, M.1    Goncalves, F.C.2    Steiner, W.3
  • 10
    • 72049114963 scopus 로고    scopus 로고
    • Multicopper oxidases: A workshop on copper coordination chemistry, electron transfer, and metallophysiology
    • D.J. Kosman Multicopper oxidases: A workshop on copper coordination chemistry, electron transfer, and metallophysiology J. Biol. Inorg. Chem. 15 2010 15 28
    • (2010) J. Biol. Inorg. Chem. , vol.15 , pp. 15-28
    • Kosman, D.J.1
  • 11
    • 33646893459 scopus 로고    scopus 로고
    • Evidence for iron channeling in the Fet3p-Ftr1p high-affinity iron uptake complex in the yeast plasma membrane
    • DOI 10.1021/bi052173c
    • E.Y. Kwok, S. Severance, and D.J. Kosman Evidence for iron channeling in the Fet3p-Ftr1p high-affinity iron uptake complex in the yeast plasma membrane Biochemistry 45 2006 6317 6327 (Pubitemid 43787799)
    • (2006) Biochemistry , vol.45 , Issue.20 , pp. 6317-6327
    • Kwok, E.Y.1    Severance, S.2    Kosman, D.J.3
  • 12
    • 65649097276 scopus 로고    scopus 로고
    • Crystal structure of a two-domain multicopper oxidase: Implications for the evolution of multicopper blue proteins
    • T.J. Lawton, L.A. Sayavedra-Soto, D.J. Arp, and A.C. Rosenzweig Crystal structure of a two-domain multicopper oxidase: Implications for the evolution of multicopper blue proteins J. Biol. Chem. 284 2009 10174 10180
    • (2009) J. Biol. Chem. , vol.284 , pp. 10174-10180
    • Lawton, T.J.1    Sayavedra-Soto, L.A.2    Arp, D.J.3    Rosenzweig, A.C.4
  • 14
    • 0004255668 scopus 로고    scopus 로고
    • World Scientific Publishing Company, Inc. Singapore
    • A. Messerschmidt Multi-Copper Oxidases 1997 World Scientific Publishing Company, Inc. Singapore
    • (1997) Multi-Copper Oxidases
    • Messerschmidt, A.1
  • 16
    • 24744433115 scopus 로고    scopus 로고
    • Function and molecular evolution of multicopper blue proteins
    • DOI 10.1007/s00018-004-5076-x
    • K. Nakamura, and N. Go Function and molecular evolution of multicopper blue proteins Cell. Mol. Life Sci. 62 2005 2050 2066 (Pubitemid 41291662)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.18 , pp. 2050-2066
    • Nakamura, K.1    Go, N.2
  • 17
    • 0142169403 scopus 로고    scopus 로고
    • Novel types of two-domain multi-copper oxidases: Possible missing links in the evolution
    • DOI 10.1016/S0014-5793(03)01000-7
    • K. Nakamura, T. Kawabata, K. Yura, and N. Go Novel types of two-domain multi-copper oxidases: Possible missing links in the evolution FEBS Lett. 553 2003 239 244 (Pubitemid 37315611)
    • (2003) FEBS Letters , vol.553 , Issue.3 , pp. 239-244
    • Nakamura, K.1    Kawabata, T.2    Yura, K.3    Go, N.4
  • 18
    • 70449116515 scopus 로고    scopus 로고
    • Structural basis of inter-protein electron transfer for nitrite reduction in denitrification
    • M. Nojiri, H. Koteishi, T. Nakagami, K. Kobayashi, T. Inoue, K. Yamaguchi, and S. Suzuki Structural basis of inter-protein electron transfer for nitrite reduction in denitrification Nature 462 2009 117 120
    • (2009) Nature , vol.462 , pp. 117-120
    • Nojiri, M.1    Koteishi, H.2    Nakagami, T.3    Kobayashi, K.4    Inoue, T.5    Yamaguchi, K.6    Suzuki, S.7
  • 20
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Macromol. Crystallogr. Pt A 276 1997 307 326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 25
    • 79955505876 scopus 로고    scopus 로고
    • (personal communication)
    • Stein, L. Y. (personal communication)
    • Stein, L.Y.1
  • 28
    • 58849150713 scopus 로고    scopus 로고
    • The Fox1 ferroxidase of Chlamydomonas reinhardtii: A new multicopper oxidase structural paradigm
    • A.J. Terzulli, and D.J. Kosman The Fox1 ferroxidase of Chlamydomonas reinhardtii: A new multicopper oxidase structural paradigm J. Biol. Inorg. Chpem. 14 2009 315 325
    • (2009) J. Biol. Inorg. Chpem. , vol.14 , pp. 315-325
    • Terzulli, A.J.1    Kosman, D.J.2
  • 29
    • 37549050579 scopus 로고    scopus 로고
    • Conformation of pseudoazurin in the 152 kDa electron transfer complex with nitrite reductase determined by paramagnetic NMR
    • M.D. Vlasie, R. Fernandez-Busnadiego, M. Prudencio, and M. Ubbink Conformation of pseudoazurin in the 152 kDa electron transfer complex with nitrite reductase determined by paramagnetic NMR J. Mol. Biol. 375 2008 1405 1415
    • (2008) J. Mol. Biol. , vol.375 , pp. 1405-1415
    • Vlasie, M.D.1    Fernandez-Busnadiego, R.2    Prudencio, M.3    Ubbink, M.4
  • 30
    • 36549027357 scopus 로고    scopus 로고
    • Automated structure solution with autoSHARP
    • DOI 10.1385/1-59745-266-1:215, Macromolecular Crystallography Protocols, Volume 2: Structure Determination
    • C. Vonrhein, E. Blanc, P. Roversi, and G. Bricogne Automated structure solution with autoSHARP S. Doubli, Methods in Molecular Biology Vol. 364 2007 Humana Press, Inc. Totowa, NJ 215 230 (Pubitemid 350183137)
    • (2007) Methods in Molecular Biology , vol.364 , pp. 215-230
    • Vonrhein, C.1    Blanc, E.2    Roversi, P.3    Bricogne, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.