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Volumn 142, Issue 3, 2007, Pages 335-341

Identification of a blue copper protein from Hyphomicrobium denitrificans and its functions in the periplasm

Author keywords

Blue copper protein; Denitrification; Electron transfer; Methylotroph; Type 1 copper

Indexed keywords

COPPER PROTEIN; CYTOCHROME C1; METHANOL;

EID: 36849012476     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvm136     Document Type: Article
Times cited : (12)

References (49)
  • 1
    • 0024270682 scopus 로고
    • Nitrate removal from a sewage by supplementation of methanol using a submerged soil column, and changes in the population of methanol-utilizing denitrifiers in the column soil
    • Aida, T. and Nomoto, K. (1988) Nitrate removal from a sewage by supplementation of methanol using a submerged soil column, and changes in the population of methanol-utilizing denitrifiers in the column soil. Jpn. J. Soil Sci. Plant Nutr. 59, 464-470
    • (1988) Jpn. J. Soil Sci. Plant Nutr , vol.59 , pp. 464-470
    • Aida, T.1    Nomoto, K.2
  • 2
    • 0015146781 scopus 로고
    • Denitrification with methanol: A selective enrichment for Hyphomicrobium species
    • Sperl, G.T. and Hoare, D.S. (1971) Denitrification with methanol: a selective enrichment for Hyphomicrobium species. J. Bacteriol. 108, 733-736
    • (1971) J. Bacteriol , vol.108 , pp. 733-736
    • Sperl, G.T.1    Hoare, D.S.2
  • 3
    • 3042691747 scopus 로고    scopus 로고
    • The quinoprotein dehydrogenases for methanol and glucose
    • Anthony, C. (2004) The quinoprotein dehydrogenases for methanol and glucose. Arch. Biochem. Biophys. 428, 2-9
    • (2004) Arch. Biochem. Biophys , vol.428 , pp. 2-9
    • Anthony, C.1
  • 4
    • 1242273667 scopus 로고    scopus 로고
    • The structure and mechanism of methanol dehydrogenase
    • Anthony, C. and Williams, P. (2003) The structure and mechanism of methanol dehydrogenase. Biochim. Biophys. Acta 1647, 18-23
    • (2003) Biochim. Biophys. Acta , vol.1647 , pp. 18-23
    • Anthony, C.1    Williams, P.2
  • 5
    • 0030442943 scopus 로고    scopus 로고
    • Quinoprotein-catalyzed reactions
    • Anthony, C. (1996) Quinoprotein-catalyzed reactions. Biochem. J. 320, 697-711
    • (1996) Biochem. J , vol.320 , pp. 697-711
    • Anthony, C.1
  • 6
    • 0002788957 scopus 로고
    • Methanol dehydrogenase in gram-negative bacteria in
    • Davidson, V. L, ed, pp, Marcel Dekker, Inc, New York
    • Anthony, C. (1993) Methanol dehydrogenase in gram-negative bacteria in. in Principles and Applications of Quinoproteins (Davidson, V. L., ed.) pp. 17-45 Marcel Dekker, Inc., New York
    • (1993) Principles and Applications of Quinoproteins , pp. 17-45
    • Anthony, C.1
  • 7
    • 0003075538 scopus 로고
    • The role of quinoproteins in bacterial energy transduction in
    • Davidson, V. L, ed, pp, Marcel Dekker, Inc, New York
    • Anthony, C. (1993) The role of quinoproteins in bacterial energy transduction in. in Principles and Applications of Quinoproteins (Davidson, V. L., ed.) pp. 223-244 Marcel Dekker, Inc., New York
    • (1993) Principles and Applications of Quinoproteins , pp. 223-244
    • Anthony, C.1
  • 8
    • 33645227940 scopus 로고    scopus 로고
    • L and methanol dehydrogenase from Hyphomicrobium denitrificans: Structural and mechanistic insights into interactions between the two proteins
    • L and methanol dehydrogenase from Hyphomicrobium denitrificans: structural and mechanistic insights into interactions between the two proteins. Biochemistry 45, 3481-3492
    • (2006) Biochemistry , vol.45 , pp. 3481-3492
    • Nojiri, M.1    Hira, D.2    Yamaguchi, K.3    Okajima, T.4    Tanizawa, K.5    Suzuki, S.6
  • 10
    • 0025103905 scopus 로고
    • Soluble cytochromes c of methanol-utilizing bacteria
    • Day, D.J. and Anthony, C. (1990) Soluble cytochromes c of methanol-utilizing bacteria. Methods Enzymol. 188, 298-303
    • (1990) Methods Enzymol , vol.188 , pp. 298-303
    • Day, D.J.1    Anthony, C.2
  • 12
    • 0037173555 scopus 로고    scopus 로고
    • Spectroscopic and functional characterization of Cu-containing nitrite reductase from Hyphomicrobium denitrificans A3151
    • Deligeer, F., R., Kataoka, K., Yamaguchi, K., Kobayashi, K., Tagawa, S., and Suzuki, S. (2002) Spectroscopic and functional characterization of Cu-containing nitrite reductase from Hyphomicrobium denitrificans A3151. J. Inorg. Biochem. 91, 132-138
    • (2002) J. Inorg. Biochem , vol.91 , pp. 132-138
    • Deligeer, F.R.1    Kataoka, K.2    Yamaguchi, K.3    Kobayashi, K.4    Tagawa, S.5    Suzuki, S.6
  • 13
    • 8444245920 scopus 로고    scopus 로고
    • Characterization of two type 1 Cu sites of Hyphomicrobium denitrificans nitrite reductase: A new class of copper-containing nitrite reductase
    • Yamaguchi, K., Kataoka, K., Kobayashi, M., Itoh, K., Fukui, A., and Suzuki, S. (2004) Characterization of two type 1 Cu sites of Hyphomicrobium denitrificans nitrite reductase: a new class of copper-containing nitrite reductase. Biochemistry 43, 14180-14188
    • (2004) Biochemistry , vol.43 , pp. 14180-14188
    • Yamaguchi, K.1    Kataoka, K.2    Kobayashi, M.3    Itoh, K.4    Fukui, A.5    Suzuki, S.6
  • 14
    • 1342304268 scopus 로고    scopus 로고
    • Characterization of nitrous oxide reductase from a methylotrophic denitrifying bacterium
    • Yamaguchi, K., Kawamura, A., Ogawa, H., and Suzuki, S. (2003) Characterization of nitrous oxide reductase from a methylotrophic denitrifying bacterium, Hyphomicrobium denitrificans. J. Biochem. 134, 853-858
    • (2003) Hyphomicrobium denitrificans. J. Biochem , vol.134 , pp. 853-858
    • Yamaguchi, K.1    Kawamura, A.2    Ogawa, H.3    Suzuki, S.4
  • 15
    • 34248387742 scopus 로고    scopus 로고
    • Nojiri, M., Xie, Y., Inoue, T., Yamamoto, T., Matsumura, H., Kataoka, K., Deligeer, Yamaguchi, K., Kai, Y., and Suzuki, S. (2007) Structure and function of a hexameric copper-containing nitrite reductase. Proc. Natl. Acad. Sci. USA 104, 4315-4320
    • Nojiri, M., Xie, Y., Inoue, T., Yamamoto, T., Matsumura, H., Kataoka, K., Deligeer, , Yamaguchi, K., Kai, Y., and Suzuki, S. (2007) Structure and function of a hexameric copper-containing nitrite reductase. Proc. Natl. Acad. Sci. USA 104, 4315-4320
  • 16
    • 0002883405 scopus 로고
    • Blue copper proteins in electron transport in methylotrophic bacteria in
    • Crawford, R.L. and Hanson, R.S, eds, pp, American Society for Microbiology, Washington
    • Tobari, J. (1984) Blue copper proteins in electron transport in methylotrophic bacteria in. in Microbial growth on C1 compounds (Crawford, R.L. and Hanson, R.S., eds.) pp. 106-112 American Society for Microbiology, Washington
    • (1984) Microbial growth on C1 compounds , pp. 106-112
    • Tobari, J.1
  • 17
    • 0022334324 scopus 로고
    • The primary structures of Pseudomonas AM1 amicyanin and pseudoazurin
    • Ambler, R.P. and Tobari, J. (1985) The primary structures of Pseudomonas AM1 amicyanin and pseudoazurin. Biochem. J. 232, 451-457
    • (1985) Biochem. J , vol.232 , pp. 451-457
    • Ambler, R.P.1    Tobari, J.2
  • 18
    • 0019891342 scopus 로고
    • Amicyanin: An electron acceptor of methylamine dehydrogenase
    • Tobari, J. and Harada, Y. (1981) Amicyanin: an electron acceptor of methylamine dehydrogenase. Biochem. Biophys. Res. Commun. 101, 502-508
    • (1981) Biochem. Biophys. Res. Commun , vol.101 , pp. 502-508
    • Tobari, J.1    Harada, Y.2
  • 19
    • 0022400803 scopus 로고
    • An inducible periplasmic blue copper protein from Paracoccus denitrificans
    • Husain, M. and Davidson, V.L. (1985) An inducible periplasmic blue copper protein from Paracoccus denitrificans. J. Biol. Chem. 260, 14626-14629
    • (1985) J. Biol. Chem , vol.260 , pp. 14626-14629
    • Husain, M.1    Davidson, V.L.2
  • 20
    • 0023043203 scopus 로고
    • Properties of Paracoccus denitrificans amicyanin
    • Husain, M., Davidson, V.L., and Smith, A.J. (1986) Properties of Paracoccus denitrificans amicyanin. Biochemistry 25, 2431-2436
    • (1986) Biochemistry , vol.25 , pp. 2431-2436
    • Husain, M.1    Davidson, V.L.2    Smith, A.J.3
  • 21
    • 0023812932 scopus 로고
    • Complex formation between methylamine dehydrogenase and amicyanin from Paracoccus denitrificans
    • Gray, K.A., Davidson, V.L., and Knaff, D.B. (1988) Complex formation between methylamine dehydrogenase and amicyanin from Paracoccus denitrificans. J. Biol. Chem. 263, 13987-13990
    • (1988) J. Biol. Chem , vol.263 , pp. 13987-13990
    • Gray, K.A.1    Davidson, V.L.2    Knaff, D.B.3
  • 23
    • 0030514355 scopus 로고    scopus 로고
    • X-ray structure of the cupredoxin amicyanin, from Paracoccus denitrificans, refined at 1.31 Å resolution
    • Cunane, L.M., Chen, Z.W., Durley, R.C.E., and Mathews, F.S. (1996) X-ray structure of the cupredoxin amicyanin, from Paracoccus denitrificans, refined at 1.31 Å resolution. Acta Crystallogr. D52, 676-686
    • (1996) Acta Crystallogr , vol.D52 , pp. 676-686
    • Cunane, L.M.1    Chen, Z.W.2    Durley, R.C.E.3    Mathews, F.S.4
  • 24
    • 0024970798 scopus 로고
    • Two distinct azurins function in the electron-transport chain of the obligate methylotroph Methylomonas J
    • Ambler, R.P. and Tobari, J. (1989) Two distinct azurins function in the electron-transport chain of the obligate methylotroph Methylomonas J. Biochem. J. 261, 495-499
    • (1989) Biochem. J , vol.261 , pp. 495-499
    • Ambler, R.P.1    Tobari, J.2
  • 25
    • 0032059760 scopus 로고    scopus 로고
    • Cloning and characterization of the azurin iso-1 gene, concerned with the electron transport chain involved in methylamine/methanol oxidation in the obligate methylotroph Methylomonas sp. strain J
    • Taguchi, K., Kudo, T., and Tobari, J. (1998) Cloning and characterization of the azurin iso-1 gene, concerned with the electron transport chain involved in methylamine/methanol oxidation in the obligate methylotroph Methylomonas sp. strain J. Biosci. Biotechnol. Biochem. 62, 870-874
    • (1998) Biosci. Biotechnol. Biochem , vol.62 , pp. 870-874
    • Taguchi, K.1    Kudo, T.2    Tobari, J.3
  • 26
    • 36849009488 scopus 로고    scopus 로고
    • Yamaguchi, K., Deligeer, Nakamura, N., Shidara, S., Iwasaki, H., and Suzuki, S. (1995) Isolation and characterization of two distinct azurins from Alcaligenes xylosoxidans subsp. xylosoxidans NCIB11015 or GIFU1051. Chem. Lett., 1995, 353-354
    • Yamaguchi, K., Deligeer, , Nakamura, N., Shidara, S., Iwasaki, H., and Suzuki, S. (1995) Isolation and characterization of two distinct azurins from Alcaligenes xylosoxidans subsp. xylosoxidans NCIB11015 or GIFU1051. Chem. Lett., 1995, 353-354
  • 28
    • 0029187321 scopus 로고
    • Structure of a new azurin from the denitrifying bacterium Alcaligenes xylosoxidans at high resolution
    • Dodd, F.E., Hasnain, S.S, Abraham, Z.H.L., Eady, R.R., and Smith, B.E. (1995) Structure of a new azurin from the denitrifying bacterium Alcaligenes xylosoxidans at high resolution. Acta Crystallogr. D51, 1052-1064
    • (1995) Acta Crystallogr , vol.D51 , pp. 1052-1064
    • Dodd, F.E.1    Hasnain, S.S.2    Abraham, Z.H.L.3    Eady, R.R.4    Smith, B.E.5
  • 29
    • 0032077185 scopus 로고    scopus 로고
    • Structure of azurin I from the denitrifying bacterium Alcaligenes xylosoxidans NCIMB 11015 at 2.45Å resolution
    • Li, C., Inoue, T., Gotowda, M., Suzuki, S., Yamaguchi, K., Kataoka, K., and Kai, Y. (1998) Structure of azurin I from the denitrifying bacterium Alcaligenes xylosoxidans NCIMB 11015 at 2.45Å resolution. Acta Crystallogr. D54, 347-354
    • (1998) Acta Crystallogr , vol.D54 , pp. 347-354
    • Li, C.1    Inoue, T.2    Gotowda, M.3    Suzuki, S.4    Yamaguchi, K.5    Kataoka, K.6    Kai, Y.7
  • 30
    • 0027974388 scopus 로고
    • Refined crystal structure of pseudoazurin from Methylobacterium extorquens AM1 at 1.5 Å resolution
    • Inoue, T., Kai, Y., Harada, S., Kasai, N., Ohshiro, Y., Suzuki, S., Kohzuma, T., and Tobari, J. (1994) Refined crystal structure of pseudoazurin from Methylobacterium extorquens AM1 at 1.5 Å resolution. Acta Crystallogr. D50, 317-328
    • (1994) Acta Crystallogr , vol.D50 , pp. 317-328
    • Inoue, T.1    Kai, Y.2    Harada, S.3    Kasai, N.4    Ohshiro, Y.5    Suzuki, S.6    Kohzuma, T.7    Tobari, J.8
  • 32
    • 0032714437 scopus 로고    scopus 로고
    • Suzuki, S., Nakamura, N., Yamaguchi, K., Kataoka, K., Inoue, T., Nshio, N., Kai, Y., and Tobari, J. (1999) Spectroscopic and electrochemical properties of two azurins (Az-iso1 and Az-iso2) from the obligate methylotroph Methyromonas sp. strain J and the structure of novel Az-iso2. J. Biol. Inorg. Chem. 4, 749-758
    • Suzuki, S., Nakamura, N., Yamaguchi, K., Kataoka, K., Inoue, T., Nshio, N., Kai, Y., and Tobari, J. (1999) Spectroscopic and electrochemical properties of two azurins (Az-iso1 and Az-iso2) from the obligate methylotroph Methyromonas sp. strain J and the structure of novel Az-iso2. J. Biol. Inorg. Chem. 4, 749-758
  • 33
    • 0002621882 scopus 로고
    • Electrochemical properties of copper proteins, pseudoazurin and nitrite reductase from Achromobacter cycloclastes IAM 1013
    • Kohzuma, T., Takase, S., Shidara, S., and Suzuki, S. (1993) Electrochemical properties of copper proteins, pseudoazurin and nitrite reductase from Achromobacter cycloclastes IAM 1013. Chem. Lett., 1993, 149-152
    • (1993) Chem. Lett , vol.1993 , pp. 149-152
    • Kohzuma, T.1    Takase, S.2    Shidara, S.3    Suzuki, S.4
  • 34
    • 0028958832 scopus 로고
    • Identification of interaction site of pseudoazurin with its redox partner, copper-containing nitrite reductase from Alcaligenes faecalis S-6
    • Kukimoto, M., Nishiyama, M., Ohnuki, T., Turley, S., Adman, E.T., and Horinouchi, S. (1995) Identification of interaction site of pseudoazurin with its redox partner, copper-containing nitrite reductase from Alcaligenes faecalis S-6. Protein Eng. 8, 153-158
    • (1995) Protein Eng , vol.8 , pp. 153-158
    • Kukimoto, M.1    Nishiyama, M.2    Ohnuki, T.3    Turley, S.4    Adman, E.T.5    Horinouchi, S.6
  • 35
    • 0029995615 scopus 로고    scopus 로고
    • Studies on protein-protein interaction between copper-containing nitrite reductase and pseudoazurin from Alcaligenes faecalis S-6
    • Kukimoto, M., Nishiyama, M., Tanokura, M., Adman, E.T., and Horinouchi, S. (1996) Studies on protein-protein interaction between copper-containing nitrite reductase and pseudoazurin from Alcaligenes faecalis S-6. J. Biol. Chem. 271, 13680-13689
    • (1996) J. Biol. Chem , vol.271 , pp. 13680-13689
    • Kukimoto, M.1    Nishiyama, M.2    Tanokura, M.3    Adman, E.T.4    Horinouchi, S.5
  • 36
    • 17944403239 scopus 로고    scopus 로고
    • Structure-function relationships of copper-containing nitrite reductases
    • Suzuki, S., Kataoka, K., Yamaguchi, K., Inoue, T., and Kai, Y. (1999) Structure-function relationships of copper-containing nitrite reductases. Coordin.. Chem. Rev. 190-192, 245-265
    • (1999) Coordin.. Chem. Rev , vol.190-192 , pp. 245-265
    • Suzuki, S.1    Kataoka, K.2    Yamaguchi, K.3    Inoue, T.4    Kai, Y.5
  • 37
    • 0024379499 scopus 로고
    • The respiratory chains of pathogenic Pseudomonas
    • Zannoni, D. (1989) The respiratory chains of pathogenic Pseudomonas. Biochim. Biophys. Acta 975, 299-316
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 299-316
    • Zannoni, D.1
  • 38
    • 0023656565 scopus 로고
    • Type 1, blue copper proteins constitute a respiratory nitrite-reducing system in Pseudomonas aureofaciens
    • Zumft, W.G., Gotzmann, D.J., and Kroneck, P.M. (1987) Type 1, blue copper proteins constitute a respiratory nitrite-reducing system in Pseudomonas aureofaciens. Eur. J. Biochem. 168, 301-307
    • (1987) Eur. J. Biochem , vol.168 , pp. 301-307
    • Zumft, W.G.1    Gotzmann, D.J.2    Kroneck, P.M.3
  • 39
    • 0030771742 scopus 로고    scopus 로고
    • In vivo studies disprove an obligatory role of azurin in denitrification in Pseudomonas aeruginosa and show that azu expression is under control of RpoS and ANR
    • Vijgenboom, E., Busch, J.E., and Canters, G.W. (1997) In vivo studies disprove an obligatory role of azurin in denitrification in Pseudomonas aeruginosa and show that azu expression is under control of RpoS and ANR. Microbiology 143, 2853-2863
    • (1997) Microbiology , vol.143 , pp. 2853-2863
    • Vijgenboom, E.1    Busch, J.E.2    Canters, G.W.3
  • 40
    • 0001205862 scopus 로고
    • Some properties of a blue copper protein 'plantacyanin' from cucumber peel
    • Sakurai, T., Okamoto, H., Kawahara, K., and Nakahara, A. (1982) Some properties of a blue copper protein 'plantacyanin' from cucumber peel. FEBS Lett. 147, 220-224
    • (1982) FEBS Lett , vol.147 , pp. 220-224
    • Sakurai, T.1    Okamoto, H.2    Kawahara, K.3    Nakahara, A.4
  • 41
    • 0032560925 scopus 로고    scopus 로고
    • Spectroscopic and geometric variations in perturbed blue copper centers: Electronic structures of stellacyanin and cucumber basic protein
    • LaCroix, L.B., Randall, D.W., Nersissian, A.M., Hoitink, C.W.G., Canters, W.G., Valentine, J.S., and Solomon, E.I. (1998) Spectroscopic and geometric variations in perturbed blue copper centers: electronic structures of stellacyanin and cucumber basic protein. J. Am. Chem. Soc. 120, 9621-9631
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 9621-9631
    • LaCroix, L.B.1    Randall, D.W.2    Nersissian, A.M.3    Hoitink, C.W.G.4    Canters, W.G.5    Valentine, J.S.6    Solomon, E.I.7
  • 42
    • 1542378734 scopus 로고    scopus 로고
    • Electronic structures of metal sites in proteins and models: Contributions to function in blue copper proteins
    • Solomon, E.I., Szilagyi, R.K., George, S.D., and Basumallick, L. (2004) Electronic structures of metal sites in proteins and models: contributions to function in blue copper proteins. Chem. Rev. 104, 419-458
    • (2004) Chem. Rev , vol.104 , pp. 419-458
    • Solomon, E.I.1    Szilagyi, R.K.2    George, S.D.3    Basumallick, L.4
  • 43
    • 0001200103 scopus 로고
    • Spectroscopic studies of stellacyanin, plastocyanin, and azurin: Electronic structure of the blue copper sites
    • Solomon, E.I., Hare, J.W., Dooley, D.M., Dawson, J.H., Stephens, P.J., and Gray, H.B. (1980) Spectroscopic studies of stellacyanin, plastocyanin, and azurin: electronic structure of the blue copper sites. J. Am. Chem. Soc. 102, 168-178
    • (1980) J. Am. Chem. Soc , vol.102 , pp. 168-178
    • Solomon, E.I.1    Hare, J.W.2    Dooley, D.M.3    Dawson, J.H.4    Stephens, P.J.5    Gray, H.B.6
  • 44
    • 0000940587 scopus 로고
    • Spectroscopic characterization of cobalt(II)-substituted Achromobacter pseudoazurin: Similarity of the metal center in Co(II)-pseudoazurin to those in Co(II)-plastocyanin and Co(II)-plantacyanin
    • Suzuki, S., Sakurai, T., Shidara, S., and Iwasaki, H. (1989) Spectroscopic characterization of cobalt(II)-substituted Achromobacter pseudoazurin: similarity of the metal center in Co(II)-pseudoazurin to those in Co(II)-plastocyanin and Co(II)-plantacyanin. Inorg. Chem. 28, 802-804
    • (1989) Inorg. Chem , vol.28 , pp. 802-804
    • Suzuki, S.1    Sakurai, T.2    Shidara, S.3    Iwasaki, H.4
  • 45
    • 0023667457 scopus 로고
    • The crystal structure of pseudoazurin from Alcaligenes faecalis S-6 determined at 2.9 Å resolution
    • Petratos, K., Banner, D.W., Beppu, T., Wilson, K.S., and Tsernoglou, D. (1987) The crystal structure of pseudoazurin from Alcaligenes faecalis S-6 determined at 2.9 Å resolution. FEBS Lett. 218, 209-214
    • (1987) FEBS Lett , vol.218 , pp. 209-214
    • Petratos, K.1    Banner, D.W.2    Beppu, T.3    Wilson, K.S.4    Tsernoglou, D.5
  • 46
    • 0000454598 scopus 로고
    • Refinement of the structure of pseudoazurin from Alcaligenes faecalis S-6 at 1.55 Å resolution
    • Petratos, K., Danter, Z., and Wilson, K.S. (1988) Refinement of the structure of pseudoazurin from Alcaligenes faecalis S-6 at 1.55 Å resolution. Acta Crystallogr. B44, 628-636
    • (1988) Acta Crystallogr , vol.B44 , pp. 628-636
    • Petratos, K.1    Danter, Z.2    Wilson, K.S.3
  • 47
    • 0024285044 scopus 로고
    • Phase determination by multiple-wavelength x-ray diffraction: Crystal structure and a basic 'blue' copper protein from cucumbers
    • Guss, J.M., Merritt, E.A., Phizackerlev, R.P., Hedman, B., Murata, M., Hodgson, K.O., and Freeman, H.C. (1988) Phase determination by multiple-wavelength x-ray diffraction: crystal structure and a basic 'blue' copper protein from cucumbers. Science 241, 806-811
    • (1988) Science , vol.241 , pp. 806-811
    • Guss, J.M.1    Merritt, E.A.2    Phizackerlev, R.P.3    Hedman, B.4    Murata, M.5    Hodgson, K.O.6    Freeman, H.C.7
  • 48
    • 13244279481 scopus 로고    scopus 로고
    • Functionally specified protein signatures distinctive for each of the different blue copper proteins
    • Giri, A.V., Anishetty, S., and Gautam, P. (2004) Functionally specified protein signatures distinctive for each of the different blue copper proteins. BMC Bioinfom 5, 127-135
    • (2004) BMC Bioinfom , vol.5 , pp. 127-135
    • Giri, A.V.1    Anishetty, S.2    Gautam, P.3
  • 49
    • 0344312436 scopus 로고    scopus 로고
    • The Paracoccus denitrificans electron transport system: Aspects of organisation, structures and biogenesis in
    • Canters, G.W. and Vijgenboom, E, eds, pp, Kluwer Academic Publishers, The Netherlands
    • Ferguson, S.J. (1998) The Paracoccus denitrificans electron transport system: aspects of organisation, structures and biogenesis in. in Biological Electron Transfer Chains: Genetics, Composition and Mode of Operation (Canters, G.W. and Vijgenboom, E., eds.) pp. 77-88 Kluwer Academic Publishers, The Netherlands
    • (1998) Biological Electron Transfer Chains: Genetics, Composition and Mode of Operation , pp. 77-88
    • Ferguson, S.J.1


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