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Volumn 390, Issue 9, 2009, Pages 863-873

A soluble form of ammonia monooxygenase in Nitrosomonas europaea

Author keywords

Acetylene; Ammonia monooxygenase (AMO); AmoA; AmoB; Copper and iron enzyme; Cytochrome c1; N terminal signal sequence; Purification

Indexed keywords

ACETYLENE; AMMONIA MONOOXYGENASE; COPPER; CYTOCHROME C1; HEME; HEMOGLOBIN GAMMA CHAIN; HYDROXYLAMINE; ISOENZYME; POTASSIUM; UNCLASSIFIED DRUG; ZINC;

EID: 70349448469     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2009.085     Document Type: Article
Times cited : (45)

References (78)
  • 1
    • 0022649451 scopus 로고
    • Tetraheme cytochrome c-554 from Nitrosomonas europaea. Heme-heme interactions and ligand binding
    • Andersson, K.K., Lipscomb, J.D., Valentine, M., Mü nck, E., and Hooper, A.B. (1986). Tetraheme cytochrome c-554 from Nitrosomonas europaea. Heme-heme interactions and ligand binding. J. Biol. Chem. 261, 1126-1138.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1126-1138
    • Andersson, K.K.1    Lipscomb, J.D.2    Valentine, M.3    Münck, E.4    Hooper, A.B.5
  • 2
    • 0036038187 scopus 로고    scopus 로고
    • Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea
    • Arp, D.J., Sayavedra-Soto, L.A., and Hommes, N.G. (2002). Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea. Arch. Microbiol. 178, 250-255.
    • (2002) Arch. Microbiol. , vol.178 , pp. 250-255
    • Arp, D.J.1    Sayavedra-Soto, L.A.2    Hommes, N.G.3
  • 3
    • 0035690880 scopus 로고    scopus 로고
    • Zinc coordination sphere in biochemical zinc sites
    • Auld, D.S. (2001). Zinc coordination sphere in biochemical zinc sites. Biometals 14, 271-313.
    • (2001) Biometals , vol.14 , pp. 271-313
    • Auld, D.S.1
  • 4
    • 34547752024 scopus 로고    scopus 로고
    • Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase
    • Balasubramanian, R. and Rosenzweig, A.C. (2007). Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase. Acc. Chem. Res. 40, 573-580.
    • (2007) Acc. Chem. Res. , vol.40 , pp. 573-580
    • Balasubramanian, R.1    Rosenzweig, A.C.2
  • 5
    • 0348087046 scopus 로고    scopus 로고
    • The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein
    • Basu, P., Katterle, B., Andersson, K.K., and Dalton, H. (2003). The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein. Biochem. J. 369, 417-427.
    • (2003) Biochem. J. , vol.369 , pp. 417-427
    • Basu, P.1    Katterle, B.2    Andersson, K.K.3    Dalton, H.4
  • 7
    • 0019248894 scopus 로고
    • Preparation of membrane vesicles in lithium chloride from cells of Nitrosomonas europaea
    • Bhandari, B. and Nicholas, D.J.D. (1980). Preparation of membrane vesicles in lithium chloride from cells of Nitrosomonas europaea. Anal. Biochem. 109, 330-337.
    • (1980) Anal. Biochem. , vol.109 , pp. 330-337
    • Bhandari, B.1    Nicholas, D.J.D.2
  • 8
    • 0016203040 scopus 로고
    • A film detection method for tritium-labeled proteins and nucleic acids in polyacrylamide gels
    • Bonner, W.M. and Laskey, R.A. (1974). A film detection method for tritium-labeled proteins and nucleic acids in polyacrylamide gels. Eur. J. Biochem. 46, 83-88.
    • (1974) Eur. J. Biochem. , vol.46 , pp. 83-88
    • Bonner, W.M.1    Laskey, R.A.2
  • 9
    • 0020771781 scopus 로고
    • Studies by e.p.r. spectroscopy of carbon monoxide oxidases from Pseudomonas carboxydovorans and Pseudomonas carboxydohydrogena
    • Bray, R.C., George, G.N., Lange, R., and Meyer, O. (1983). Studies by e.p.r. spectroscopy of carbon monoxide oxidases from Pseudomonas carboxydovorans and Pseudomonas carboxydohydrogena. Biochem. J. 211, 687-694.
    • (1983) Biochem. J. , vol.211 , pp. 687-694
    • Bray, R.C.1    George, G.N.2    Lange, R.3    Meyer, O.4
  • 11
    • 4644230771 scopus 로고    scopus 로고
    • Toward delineating the structure and function of the particulate methane monooxygenase from methanotrophic bacteria
    • Chan, S.I., Chen, K.H.-C., Yu, S.S.-F., Chen, C.-L., and Kuo, S.S.-J. (2004). Toward delineating the structure and function of the particulate methane monooxygenase from methanotrophic bacteria. Biochemistry 43, 4421-4430.
    • (2004) Biochemistry , vol.43 , pp. 4421-4430
    • Chan, S.I.1    Chen, K.H.-C.2    Yu, S.S.-F.3    Chen, C.-L.4    Kuo, S.S.-J.5
  • 12
    • 4544332259 scopus 로고    scopus 로고
    • O2 activation by binuclear Cu sites: Noncoupled versus exchange coupled reaction mechanisms
    • Chen, P. and Solomon, E.I. (2004). O2 activation by binuclear Cu sites: noncoupled versus exchange coupled reaction mechanisms. Proc. Natl. Acad. Sci. USA 101, 13105-13110.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13105-13110
    • Chen, P.1    Solomon, E.I.2
  • 13
    • 33645849843 scopus 로고    scopus 로고
    • Theoretical modeling of the hydroxylation of methane as mediated by the particulate methane monooxygenase
    • Chen, P.P. and Chan, S.I. (2006). Theoretical modeling of the hydroxylation of methane as mediated by the particulate methane monooxygenase. J. Inorg. Biochem. 100, 801-809.
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 801-809
    • Chen, P.P.1    Chan, S.I.2
  • 14
    • 35548932041 scopus 로고    scopus 로고
    • Facile O-atom insertion into C-C and C-H bonds by a trinuclear copper complex designed to harness a singlet oxene
    • Chen, P.P., Yang, R.B., Lee, J.C., and Chan, S.I. (2007). Facile O-atom insertion into C-C and C-H bonds by a trinuclear copper complex designed to harness a singlet oxene. Proc. Natl. Acad. Sci. USA 104, 14570-14575.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 14570-14575
    • Chen, P.P.1    Yang, R.B.2    Lee, J.C.3    Chan, S.I.4
  • 16
    • 49549085961 scopus 로고    scopus 로고
    • The assembly of membrane proteins into complexes
    • Daley, O.D. (2008). The assembly of membrane proteins into complexes. Curr. Opin. Struct. Biol. 18, 420-424.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 420-424
    • Daley, O.D.1
  • 17
    • 0002936936 scopus 로고
    • Structure and mechanism of action of the hydroxylase of soluble methane monooxygenase
    • J.C. Murrell and D.P. Kelly, eds. (Andover, UK: Intercept Press)
    • Dalton, H., Wilkins, P., and Jiang, Y. (1993). Structure and mechanism of action of the hydroxylase of soluble methane monooxygenase. In: Microbial Growth on C1 Compounds, J.C. Murrell and D.P. Kelly, eds. (Andover, UK: Intercept Press), pp. 65-80.
    • (1993) Microbial Growth on C1 Compounds , pp. 65-80
    • Dalton, H.1    Wilkins, P.2    Jiang, Y.3
  • 18
    • 0027534951 scopus 로고
    • In vitro activation of ammonia monooxygenase from Nitrosomonas europaea by copper
    • Ensign, S.A., Hyman, M.R., and Arp, D.J. (1993). In vitro activation of ammonia monooxygenase from Nitrosomonas europaea by copper. J. Bacteriol. 175, 1971-1980.
    • (1993) J. Bacteriol. , vol.175 , pp. 1971-1980
    • Ensign, S.A.1    Hyman, M.R.2    Arp, D.J.3
  • 20
    • 0037067843 scopus 로고    scopus 로고
    • The Glaser reaction mechanism. A DFT study
    • Fomina, L., Vazquez, B., Tkatchouk, E., and Fomine, S. (2002). The Glaser reaction mechanism. A DFT study. Tetrahedron 58, 6741-6747.
    • (2002) Tetrahedron , vol.58 , pp. 6741-6747
    • Fomina, L.1    Vazquez, B.2    Tkatchouk, E.3    Fomine, S.4
  • 21
    • 0026530503 scopus 로고
    • The bioenergetics of ammonia and hydroxylamine oxidation in Nitrosomonas europaea at acid and alkaline pH
    • Frijlink, M., Abee, T., Laanbrock, H.J., de Boer, W., and Konings, W.N. (1992). The bioenergetics of ammonia and hydroxylamine oxidation in Nitrosomonas europaea at acid and alkaline pH. Arch. Microbiol. 157, 194-199.
    • (1992) Arch. Microbiol. , vol.157 , pp. 194-199
    • Frijlink, M.1    Abee, T.2    Laanbrock, H.J.3    De Boer, W.4    Konings, W.N.5
  • 22
    • 61449137869 scopus 로고    scopus 로고
    • Interaction of the mechanism-based inactivator acetylene with ammonia monooxygenase of Nitrosomonas europaea
    • Gilch, S., Vogel, M., Lorenz, M.W., Meyer, O., and Schmidt, I. (2009). Interaction of the mechanism-based inactivator acetylene with ammonia monooxygenase of Nitrosomonas europaea. Microbiology 155, 279-284.
    • (2009) Microbiology , vol.155 , pp. 279-284
    • Gilch, S.1    Vogel, M.2    Lorenz, M.W.3    Meyer, O.4    Schmidt, I.5
  • 24
    • 0032146943 scopus 로고    scopus 로고
    • Effect of molybdate and tungstate on the biosynthesis of CO dehydrogenase and the molybdopterin cytosine-dinucleotide-type of molybdenum cofactor in Hydrogenophaga pseudoflava
    • Hänzelmann, P. and Meyer, O. (1998). Effect of molybdate and tungstate on the biosynthesis of CO dehydrogenase and the molybdopterin cytosine-dinucleotide-type of molybdenum cofactor in Hydrogenophaga pseudoflava. Eur. J. Biochem. 255, 755-765.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 755-765
    • Hänzelmann, P.1    Meyer, O.2
  • 25
    • 0032478599 scopus 로고    scopus 로고
    • The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing threesubunit enzyme
    • Hiep-Hoa, T., Nguyen, S.J.E., Yip, J.H., and Chan, S.I. (1997). The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing threesubunit enzyme. J. Biol. Chem. 273, 7957-7966.
    • (1997) J. Biol. Chem. , vol.273 , pp. 7957-7966
    • Hiep-Hoa, T.1    Nguyen, S.J.E.2    Yip, J.H.3    Chan, S.I.4
  • 26
    • 15644373219 scopus 로고    scopus 로고
    • Mutagenesis and expression of amo, which codes for ammonia monooxygenase in Nitrosomonas europaea
    • Hommes, N.G., Sayavedra-Soto, L.A., and Arp, D.J. (1998). Mutagenesis and expression of amo, which codes for ammonia monooxygenase in Nitrosomonas europaea. J. Bacteriol. 180, 3353-3359.
    • (1998) J. Bacteriol. , vol.180 , pp. 3353-3359
    • Hommes, N.G.1    Sayavedra-Soto, L.A.2    Arp, D.J.3
  • 27
    • 0035152075 scopus 로고    scopus 로고
    • Transcript analysis of multiple copies of amo (encoding ammonia monooxygenase) and hao (encoding hydroxylamine oxidoreductase) in Nitrosomonas europaea
    • Hommes, N.G., Sayavedra-Soto, L.A., and Arp, D.J. (2001). Transcript analysis of multiple copies of amo (encoding ammonia monooxygenase) and hao (encoding hydroxylamine oxidoreductase) in Nitrosomonas europaea. J. Bacteriol. 183, 1096-1100.
    • (2001) J. Bacteriol. , vol.183 , pp. 1096-1100
    • Hommes, N.G.1    Sayavedra-Soto, L.A.2    Arp, D.J.3
  • 28
    • 0015802489 scopus 로고
    • Specific inhibitor of ammonia oxidation in Nitrosomonas
    • Hooper, A.B. and Terry, K.R. (1973). Specific inhibitor of ammonia oxidation in Nitrosomonas. J. Bacteriol. 115, 480-485.
    • (1973) J. Bacteriol. , vol.115 , pp. 480-485
    • Hooper, A.B.1    Terry, K.R.2
  • 30
    • 0022065534 scopus 로고
    • Suicidal inactivation and labeling of ammonia monooxygenase by acetylene
    • Hyman, M.R. and Wood, P.M. (1985). Suicidal inactivation and labeling of ammonia monooxygenase by acetylene. Biochem. J. 227, 719-725.
    • (1985) Biochem. J. , vol.227 , pp. 719-725
    • Hyman, M.R.1    Wood, P.M.2
  • 31
    • 0025043946 scopus 로고
    • The small-scale production of wU-14Cxacetylene from Baw14CxO3: Application to labeling of ammonia monooxygenase in autotrophic nitrifying bacteria
    • Hyman, M.R. and Arp, D.J. (1990). The small-scale production of wU-14Cxacetylene from Baw14CxO3: application to labeling of ammonia monooxygenase in autotrophic nitrifying bacteria. Anal. Biochem. 190, 348-353.
    • (1990) Anal. Biochem. , vol.190 , pp. 348-353
    • Hyman, M.R.1    Arp, D.J.2
  • 32
    • 0027165601 scopus 로고
    • An electrophoretic study of the thermal- and reductant-dependent aggregation of the 27 kDa component of ammonia monooxygenase from Nitrosomonas europaea
    • Hyman, M.R. and Arp, D.J. (1993). An electrophoretic study of the thermal- and reductant-dependent aggregation of the 27 kDa component of ammonia monooxygenase from Nitrosomonas europaea. Electrophoresis 14, 619-627.
    • (1993) Electrophoresis , vol.14 , pp. 619-627
    • Hyman, M.R.1    Arp, D.J.2
  • 33
    • 0018159772 scopus 로고
    • Inhibition by acetylene of ammonia oxidation in Nitrosomonas europaea
    • Hynes, R.K. and Knowles, R. (1978). Inhibition by acetylene of ammonia oxidation in Nitrosomonas europaea. FEMS Microbiol. Lett. 4, 319-321.
    • (1978) FEMS Microbiol. Lett. , vol.4 , pp. 319-321
    • Hynes, R.K.1    Knowles, R.2
  • 34
    • 0029143426 scopus 로고
    • Roles of bovine serum albumin and copper in the assay and stability of ammonia monooxygenase activity in vitro
    • Juliette, L.J., Hyman, M.R., and Arp, D.J. (1995). Roles of bovine serum albumin and copper in the assay and stability of ammonia monooxygenase activity in vitro. J. Bacteriol. 177, 4908-4913.
    • (1995) J. Bacteriol. , vol.177 , pp. 4908-4913
    • Juliette, L.J.1    Hyman, M.R.2    Arp, D.J.3
  • 35
    • 0017855746 scopus 로고
    • Effects of phospholipids on L-lactate dehydrogenase from membranes of Escherichia coli. Activation and stabilization of the enzyme with phospholipids
    • Kimura, H. and Futai, M. (1978). Effects of phospholipids on L-lactate dehydrogenase from membranes of Escherichia coli. Activation and stabilization of the enzyme with phospholipids. J. Biol. Chem. 253, 1095-1110.
    • (1978) J. Biol. Chem. , vol.253 , pp. 1095-1110
    • Kimura, H.1    Futai, M.2
  • 36
    • 0021796811 scopus 로고
    • Bacterial ammonia transport
    • Kleiner, D. (1985). Bacterial ammonia transport. FEMS Microbiol. Rev. 32, 87-100.
    • (1985) FEMS Microbiol. Rev. , vol.32 , pp. 87-100
    • Kleiner, D.1
  • 37
    • 0031007617 scopus 로고    scopus 로고
    • A gene encoding a membrane protein exists upstream of the amoA/ amoB genes in ammonia oxidizing bacteria: A third member of the amo operon?
    • Klotz, M.G., Alzerreca, J., and Norton, J.M. (1997). A gene encoding a membrane protein exists upstream of the amoA/ amoB genes in ammonia oxidizing bacteria: a third member of the amo operon? FEMS Microbiol. Lett. 150, 65-73.
    • (1997) FEMS Microbiol. Lett. , vol.150 , pp. 65-73
    • Klotz, M.G.1    Alzerreca, J.2    Norton, J.M.3
  • 38
    • 33644560315 scopus 로고    scopus 로고
    • Optimisation of a 2-D gel electrophoresis protocol for the human-pathogenic fungus Aspergillus fumigatus
    • Kniemeyer, O., Lessing, F., Scheibner, O., Hertweck, C., and Brakhage, A.A. (2006). Optimisation of a 2-D gel electrophoresis protocol for the human-pathogenic fungus Aspergillus fumigatus. Curr. Genet. 49, 178-189.
    • (2006) Curr. Genet. , vol.49 , pp. 178-189
    • Kniemeyer, O.1    Lessing, F.2    Scheibner, O.3    Hertweck, C.4    Brakhage, A.A.5
  • 39
    • 29444459398 scopus 로고    scopus 로고
    • Multi-step assembly pathway of the cbb3-type cytochrome c oxidase complex
    • Kulajta, C., Thumfart, J.O., Haid, S., Daldal, F., and Koch, H.-G. (2006). Multi-step assembly pathway of the cbb3-type cytochrome c oxidase complex. J. Mol. Biol. 355, 989-1004.
    • (2006) J. Mol. Biol. , vol.355 , pp. 989-1004
    • Kulajta, C.1    Thumfart, J.O.2    Haid, S.3    Daldal, F.4    Koch, H.-G.5
  • 40
    • 0020641327 scopus 로고
    • Proton electrochemical gradient in washed cells of Nitrosomonas europaea and Nitrobacter agilis
    • Kumar, S. and Nicholas, D.J.D. (1983). Proton electrochemical gradient in washed cells of Nitrosomonas europaea and Nitrobacter agilis. J. Bacteriol. 154, 65-71.
    • (1983) J. Bacteriol. , vol.154 , pp. 65-71
    • Kumar, S.1    Nicholas, D.J.D.2
  • 41
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 42
    • 84931400063 scopus 로고
    • Cytochromes, R. Barrett and J. Lemberg, eds. (London/New York: Academic Press)
    • Lemberg, R. and Barrett, J. (1973). Bacterial cytochromes and cytochromes oxidases. In: Cytochromes, R. Barrett and J. Lemberg, eds. (London/New York: Academic Press), pp. 217-326.
    • (1973) Bacterial Cytochromes and Cytochromes Oxidases , pp. 217-326
    • Lemberg, R.1    Barrett, J.2
  • 43
    • 15044356424 scopus 로고    scopus 로고
    • Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane
    • Lieberman, R.L. and Rosenzweig, A.C. (2005). Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane. Nature 434, 177-182.
    • (2005) Nature , vol.434 , pp. 177-182
    • Lieberman, R.L.1    Rosenzweig, A.C.2
  • 44
    • 0028090067 scopus 로고
    • Biochemistry of the soluble methane monooxygenase
    • Lipscomb, J.D. (1994). Biochemistry of the soluble methane monooxygenase. Annu. Rev. Microbiol. 48, 371-399.
    • (1994) Annu. Rev. Microbiol. , vol.48 , pp. 371-399
    • Lipscomb, J.D.1
  • 45
    • 0001780556 scopus 로고
    • The influence of metal ion concentrations and pH value on the growth of a Nitrosomonas strain isolated from activated sludge
    • Loveless, J.E. and Painter, H.A. (1968). The influence of metal ion concentrations and pH value on the growth of a Nitrosomonas strain isolated from activated sludge. J. Gen. Microbiol. 52, 1-14.
    • (1968) J. Gen. Microbiol. , vol.52 , pp. 1-14
    • Loveless, J.E.1    Painter, H.A.2
  • 46
    • 1942536490 scopus 로고    scopus 로고
    • Interaction of cytochrome c with cytochrome oxidase: Two different docking scenarios
    • Maneg, O., Malatesta, F., Ludwig, B., and Drosou, V. (2004). Interaction of cytochrome c with cytochrome oxidase: two different docking scenarios. Biochim. Biophys. Acta 1655, 274-281.
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 274-281
    • Maneg, O.1    Malatesta, F.2    Ludwig, B.3    Drosou, V.4
  • 47
    • 37549052557 scopus 로고    scopus 로고
    • Mössbauer studies of the membrane-associated methane monooxygenase from Methylococcus capsulatus Bath: Evidence for a diiron center
    • Martinho, M., Choi, D.W., DiSpirito, A.A., Antholine, W.E., Semrau, J.D., and Mü nck, E. (2007). Mö ssbauer studies of the membrane-associated methane monooxygenase from Methylococcus capsulatus Bath: evidence for a diiron center. J. Am. Chem. Soc. 129, 15783-15785.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15783-15785
    • Martinho, M.1    Choi, D.W.2    Dispirito, A.A.3    Antholine, W.E.4    Semrau, J.D.5    Münck, E.6
  • 48
    • 0027153142 scopus 로고
    • Sequence of the gene coding for ammonia monooxygenase in Nitrosomonas europaea
    • McTavish, H., Fuchs, J.A., and Hooper, A.B. (1993). Sequence of the gene coding for ammonia monooxygenase in Nitrosomonas europaea. J. Bacteriol. 175, 2436-2444.
    • (1993) J. Bacteriol. , vol.175 , pp. 2436-2444
    • McTavish, H.1    Fuchs, J.A.2    Hooper, A.B.3
  • 49
    • 0020365905 scopus 로고
    • Characterization of the c-type cytochromes of Nitrosomonas europaea with the aid of fluorescent gels
    • Miller, D.J. and Wood, P.M. (1982). Characterization of the c-type cytochromes of Nitrosomonas europaea with the aid of fluorescent gels. Biochem. J. 207, 511-517.
    • (1982) Biochem. J. , vol.207 , pp. 511-517
    • Miller, D.J.1    Wood, P.M.2
  • 50
    • 0032478599 scopus 로고    scopus 로고
    • The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme. Isolation and characterization
    • Nguyen, H.H., Elliott, S.J., Yip, J.H., and Chan, S.I. (1998). The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme. Isolation and characterization. J. Biol. Chem. 273, 7957-7966.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7957-7966
    • Nguyen, H.H.1    Elliott, S.J.2    Yip, J.H.3    Chan, S.I.4
  • 51
    • 0031603460 scopus 로고    scopus 로고
    • Prediction of signal peptides and signal anchors by a hidden Markov model
    • Nielsen, H. and Krogh, A. (1998). Prediction of signal peptides and signal anchors by a hidden Markov model. Proc. Int. Conf. Intell. Syst. Mol. Biol. 6, 122-130.
    • (1998) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.6 , pp. 122-130
    • Nielsen, H.1    Krogh, A.2
  • 52
    • 0030753674 scopus 로고    scopus 로고
    • Copperdependent reciprocal transcriptional regulation of methane monooxygenase genes in Methylococcus capsulatus and Methylosinus trichosporium
    • Nielsen, A.K., Gerdes, K., and Murrell, J.C. (1997). Copperdependent reciprocal transcriptional regulation of methane monooxygenase genes in Methylococcus capsulatus and Methylosinus trichosporium. Mol. Microbiol. 25, 399-409.
    • (1997) Mol. Microbiol. , vol.25 , pp. 399-409
    • Nielsen, A.K.1    Gerdes, K.2    Murrell, J.C.3
  • 53
    • 0028151542 scopus 로고
    • A super-family of medium-chain-dehydrogenases/reductases (MDR). Sublines including zeta-crystallin, alcohol and polyol dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and other proteins
    • Persson, B., Zigler, J.S., and Jö rnvall, H. (1994). A super-family of medium-chain dehydrogenases/reductases (MDR). Sublines including zeta-crystallin, alcohol and polyol dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and other proteins. Eur. J. Biochem. 226, 15-22.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 15-22
    • Persson, B.1    Zigler, J.S.2    Jörnvall, H.3
  • 54
    • 0014014207 scopus 로고
    • Incorporation of atmospheric oxygen into nitrite formed during ammonia oxidation by Nitrosomonas europaea
    • Rees, M. and Nason, A. (1966). Incorporation of atmospheric oxygen into nitrite formed during ammonia oxidation by Nitrosomonas europaea. Biochem. Biophys. Acta 113, 398-401.
    • (1966) Biochem. Biophys. Acta , vol.113 , pp. 398-401
    • Rees, M.1    Nason, A.2
  • 56
    • 4444347536 scopus 로고    scopus 로고
    • Blue native electrophoresis
    • G. von Jagow and H. Schägger, eds. (Amsterdam, Netherlands: Academic Press)
    • Schägger, H. (2003). Blue native electrophoresis. In: Membrane Protein Purification and Crystallization: A Practical Guide, G. von Jagow and H. Schägger, eds. (Amsterdam, Netherlands: Academic Press), pp. 105-130.
    • (2003) Membrane Protein Purification and Crystallization: A Practical Guide , pp. 105-130
    • Schägger, H.1
  • 57
    • 0030941542 scopus 로고    scopus 로고
    • Anaerobic ammonia oxidation with nitrogen dioxide by Nitrosomonas eutropha
    • Schmidt, I. and Bock, E. (1997). Anaerobic ammonia oxidation with nitrogen dioxide by Nitrosomonas eutropha. Arch. Microbiol. 167, 106-111.
    • (1997) Arch. Microbiol. , vol.167 , pp. 106-111
    • Schmidt, I.1    Bock, E.2
  • 58
    • 0031662047 scopus 로고    scopus 로고
    • Anaerobic ammonia oxidation by cell-free extracts of Nitrosomonas eutropha
    • Schmidt, I. and Bock, E. (1998). Anaerobic ammonia oxidation by cell-free extracts of Nitrosomonas eutropha. Antonie van Leeuwenhoek 73, 271-278.
    • (1998) Antonie Van Leeuwenhoek , vol.73 , pp. 271-278
    • Schmidt, I.1    Bock, E.2
  • 59
    • 32544456979 scopus 로고    scopus 로고
    • Anaerobic oxidation of inorganic nitrogen compounds
    • M.M. Nakano and P. Zuber, eds. (Heidelberg, Germany: Springer Horizon Scientific Press)
    • Schmidt, I. and Jetten, M.S.M. (2004). Anaerobic oxidation of inorganic nitrogen compounds. In: Strict and Facultative Anaerobes: Medical and Environmental Aspects, M.M. Nakano and P. Zuber, eds. (Heidelberg, Germany: Springer Horizon Scientific Press), pp. 283-303.
    • (2004) Strict and Facultative Anaerobes: Medical and Environmental Aspects , pp. 283-303
    • Schmidt, I.1    Jetten, M.S.M.2
  • 60
    • 0034871540 scopus 로고    scopus 로고
    • Ammonia oxidation by Nitrosomonas eutropha with NO2 as oxidant is not inhibited by acetylene
    • Schmidt, I., Bock, E., and Jetten, M.S.M. (2001). Ammonia oxidation by Nitrosomonas eutropha with NO2 as oxidant is not inhibited by acetylene. Microbiology 147, 2247-2253.
    • (2001) Microbiology , vol.147 , pp. 2247-2253
    • Schmidt, I.1    Bock, E.2    Jetten, M.S.M.3
  • 61
    • 1942475411 scopus 로고    scopus 로고
    • Physiologic and proteomic evidence for a role of nitric oxide in biofilm formation by Nitrosomonas europaea and other ammonia oxidizers
    • Schmidt, I., Steenbakkers, P.J.M., op den Camp, H.J.M., Schmidt, K., and Jetten, M.S.M. (2004). Physiologic and proteomic evidence for a role of nitric oxide in biofilm formation by Nitrosomonas europaea and other ammonia oxidizers. J. Bacteriol. 186, 2781-2788.
    • (2004) J. Bacteriol. , vol.186 , pp. 2781-2788
    • Schmidt, I.1    Steenbakkers, P.J.M.2    Op Den Camp, H.J.M.3    Schmidt, K.4    Jetten, M.S.M.5
  • 62
    • 0017662664 scopus 로고
    • High affinity lipid binding sites on the peripheral membrane enzyme pyruvate oxidase. Specific ligand effects on detergent binding
    • Schrock, H.L. and Gennis, R.B. (1977). High affinity lipid binding sites on the peripheral membrane enzyme pyruvate oxidase. Specific ligand effects on detergent binding. J. Biol. Chem. 252, 5990-5995.
    • (1977) J. Biol. Chem. , vol.252 , pp. 5990-5995
    • Schrock, H.L.1    Gennis, R.B.2
  • 63
    • 0029072153 scopus 로고
    • The role of copper in the pMMO of Methylococcus capsulatus (Bath): A structural vs. catalytic function
    • Semrau, J.D., Zolandz, D., Lidstrom, M.E., and Chan, S.I. (1995). The role of copper in the pMMO of Methylococcus capsulatus (Bath): a structural vs. catalytic function. J. Inorg. Biochem. 58, 235-244.
    • (1995) J. Inorg. Biochem. , vol.58 , pp. 235-244
    • Semrau, J.D.1    Zolandz, D.2    Lidstrom, M.E.3    Chan, S.I.4
  • 64
    • 0014933441 scopus 로고
    • Cell-free ammonia oxidation by Nitrosomonas europaea extracts: Effects of polyamines, Mg2q and albumin
    • Suzuki, I. and Kwok, S.C. (1970). Cell-free ammonia oxidation by Nitrosomonas europaea extracts: effects of polyamines, Mg2q and albumin. Biochem. Biophys. Res. Commun. 39, 950-955.
    • (1970) Biochem. Biophys. Res. Commun. , vol.39 , pp. 950-955
    • Suzuki, I.1    Kwok, S.C.2
  • 65
    • 0016197874 scopus 로고
    • Ammonia or ammonium ion as substrate for oxidation by Nitrosomonas europaea cells and extracts
    • Suzuki, I. and Kwok, S.C. (1974). Ammonia or ammonium ion as substrate for oxidation by Nitrosomonas europaea cells and extracts. J. Bacteriol. 120, 556-558.
    • (1974) J. Bacteriol. , vol.120 , pp. 556-558
    • Suzuki, I.1    Kwok, S.C.2
  • 66
    • 0019800297 scopus 로고
    • Cellfree ammonia oxidizing system of Nitrosomonas europaea: General conditions and properties
    • Suzuki, I., Kwok, S.C., Dular, U., and Tsang, D.C.Y. (1981). Cellfree ammonia oxidizing system of Nitrosomonas europaea: general conditions and properties. Can. J. Biochem. 59, 477-483.
    • (1981) Can. J. Biochem. , vol.59 , pp. 477-483
    • Suzuki, I.1    Kwok, S.C.2    Dular, U.3    Tsang, D.C.Y.4
  • 67
    • 38049165849 scopus 로고    scopus 로고
    • The product of uncI gene in F1F0-ATP synthase operon plays a chaperone-like role to assist c-ring assembly
    • Suzuki, T., Ozaki, Y., Sone, N., Feniouk, B.A., and Yosida, M. (2007). The product of uncI gene in F1F0-ATP synthase operon plays a chaperone-like role to assist c-ring assembly. Proc. Natl. Acad. Sci. USA 104, 20776-20781.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20776-20781
    • Suzuki, T.1    Ozaki, Y.2    Sone, N.3    Feniouk, B.A.4    Yosida, M.5
  • 68
    • 0034311053 scopus 로고    scopus 로고
    • Role of iron and copper in particulate methane monooxygenase of Methylosinus trichosporium OB3b
    • Takeguchi, M. and Okura, I. (2000). Role of iron and copper in particulate methane monooxygenase of Methylosinus trichosporium OB3b. Catalysis Surveys 4, 51-63.
    • (2000) Catalysis Surveys , vol.4 , pp. 51-63
    • Takeguchi, M.1    Okura, I.2
  • 69
    • 42149178708 scopus 로고    scopus 로고
    • The binuclear iron site of membrane-bound methane hydroxylase from Methylococcus capsulatus (strain M)
    • Tumanova, L.V., Tukhvatullin, I.A., Burbaev, D.S., Gvozdev, R.I., and Andersson, K.K. (2008). The binuclear iron site of membrane-bound methane hydroxylase from Methylococcus capsulatus (strain M). Russ. J. Bioorg. Chem. 34, 194-203.
    • (2008) Russ. J. Bioorg. Chem. , vol.34 , pp. 194-203
    • Tumanova, L.V.1    Tukhvatullin, I.A.2    Burbaev, D.S.3    Gvozdev, R.I.4    Andersson, K.K.5
  • 70
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • Vallee, B.L. and Falchuk, K.H. (1993). The biochemical basis of zinc physiology. Physiol. Rev. 73, 79-118.
    • (1993) Physiol. Rev. , vol.73 , pp. 79-118
    • Vallee, B.L.1    Falchuk, K.H.2
  • 71
    • 34447525672 scopus 로고    scopus 로고
    • Functional and physiological evidence for a Rhesus-type ammonia transporter in N. europaea
    • Weidinger, K., Neuhäuser, B., Gilch, S., Ludewig, U., Meyer, O., and Schmidt, I. (2007). Functional and physiological evidence for a Rhesus-type ammonia transporter in N. europaea. FEMS Microbiol. Lett. 273, 260-267.
    • (2007) FEMS Microbiol. Lett. , vol.273 , pp. 260-267
    • Weidinger, K.1    Neuhäuser, B.2    Gilch, S.3    Ludewig, U.4    Meyer, O.5    Schmidt, I.6
  • 72
    • 0018336744 scopus 로고
    • The assembly of proteins into biological membranes: The membrane trigger hypothesis
    • Wickner, W. (1979). The assembly of proteins into biological membranes: the membrane trigger hypothesis. Annu. Rev. Biochem. 48, 23-45.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 23-45
    • Wickner, W.1
  • 73
    • 0031414412 scopus 로고    scopus 로고
    • Crystal structures of the coppercontaining amine oxidase from Arthrobacter globiformis in the holo and apo forms: Implications for the biogensis of topaquine
    • Wilce, M.C.J., Dooley, D.M., Freeman, H.C., Guss, J.M., Matsunami, H., McIntire, W.S., Ruggiero, C.E., Tanizawa, K., and Yamaguchi, H. (1997). Crystal structures of the coppercontaining amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogensis of topaquine. Biochemistry 36, 16116-16133.
    • (1997) Biochemistry , vol.36 , pp. 16116-16133
    • Wilce, M.C.J.1    Dooley, D.M.2    Freeman, H.C.3    Guss, J.M.4    Matsunami, H.5    McIntire, W.S.6    Ruggiero, C.E.7    Tanizawa, K.8    Yamaguchi, H.9
  • 74
    • 0003140215 scopus 로고
    • Nitrification, J.I. Prosser, ed. (Washington, DC, USA: IRL Press)
    • Wood, P.M. (1986). Nitrification as a bacterial energy source. In: Nitrification, J.I. Prosser, ed. (Washington, DC, USA: IRL Press), pp. 39-62.
    • (1986) Nitrification As A Bacterial Energy Source , pp. 39-62
    • Wood, P.M.1
  • 75
    • 0016163720 scopus 로고
    • Cytochrome c-552 and cytochrome c-554 derived from Nitrosomonas europaea. Purification, properties, and their function in hydroxylamine oxidation
    • Yamanaka, T. and Shinra, M. (1974). Cytochrome c-552 and cytochrome c-554 derived from Nitrosomonas europaea. Purification, properties, and their function in hydroxylamine oxidation. J. Biochem. 75, 1265-1273.
    • (1974) J. Biochem. , vol.75 , pp. 1265-1273
    • Yamanaka, T.1    Shinra, M.2
  • 76
    • 0345355219 scopus 로고    scopus 로고
    • Concentration of Cu, EPR-detectable Cu, and formation of cupricferrocyanide in membranes with pMMO
    • Yuan, H., Collins, M.L., and Antholine, W.E. (1998). Concentration of Cu, EPR-detectable Cu, and formation of cupricferrocyanide in membranes with pMMO. J. Inorg. Biochem. 72, 179-185.
    • (1998) J. Inorg. Biochem. , vol.72 , pp. 179-185
    • Yuan, H.1    Collins, M.L.2    Antholine, W.E.3
  • 77
    • 0030067648 scopus 로고    scopus 로고
    • Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath)
    • Zahn, J.A. and DiSpirito, A.A. (1996). Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath). J. Bacteriol. 178, 1018-1029.
    • (1996) J. Bacteriol. , vol.178 , pp. 1018-1029
    • Zahn, J.A.1    Dispirito, A.A.2
  • 78
    • 0030580284 scopus 로고    scopus 로고
    • Evidence for an iron center in the ammonia monooxygenase from Nitrosomonas europaea
    • Zahn, J.A., Arciero, D.M., Hooper, A.B., and DiSpirito, A.A. (1996). Evidence for an iron center in the ammonia monooxygenase from Nitrosomonas europaea. FEBS Lett. 397, 35-38.
    • (1996) FEBS Lett. , vol.397 , pp. 35-38
    • Zahn, J.A.1    Arciero, D.M.2    Hooper, A.B.3    Dispirito, A.A.4


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