메뉴 건너뛰기




Volumn 43, Issue 32, 2004, Pages 10467-10474

Bidirectional catalysis by copper-containing nitrite reductase

Author keywords

[No Author keywords available]

Indexed keywords

COPPER; ELECTRONS; ENZYMES; REACTION KINETICS; SPECTROSCOPIC ANALYSIS;

EID: 4143056986     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0496687     Document Type: Article
Times cited : (57)

References (64)
  • 1
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and molecular basis of denitrification
    • Zumft, W. G. (1997) Cell biology and molecular basis of denitrification, Microbiol. Mol. Biol. Rev. 61, 533-616.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 533-616
    • Zumft, W.G.1
  • 2
    • 17944403239 scopus 로고    scopus 로고
    • Structure-function relationships of copper-containing nitrite reductases
    • Suzuki, S., Kataoke, K., Yamaguchi, K., Inoue, T., and Kai, Y. (1999) Structure-function relationships of copper-containing nitrite reductases, Coord. Chem. Rev. 190-192, 245-265.
    • (1999) Coord. Chem. Rev. , vol.190-192 , pp. 245-265
    • Suzuki, S.1    Kataoke, K.2    Yamaguchi, K.3    Inoue, T.4    Kai, Y.5
  • 3
    • 0026411154 scopus 로고
    • Copper protein structures
    • Adman, E. T. (1991) Copper protein structures. Adv. Protein Chem. 42, 145-197.
    • (1991) Adv. Protein Chem. , vol.42 , pp. 145-197
    • Adman, E.T.1
  • 4
    • 0034967182 scopus 로고    scopus 로고
    • Purification, characterization, and genetic analysis of Cu-containing dissimilatory nitrite reductase from a denitrifying halophilic archaeon, Haloarcula marismortui
    • Ichiki, H., Tanaka, Y., Mochizuki, K., Yoshimatsu, K., Sakurai, T., and Fujiwara, T. (2001) Purification, characterization, and genetic analysis of Cu-containing dissimilatory nitrite reductase from a denitrifying halophilic archaeon, Haloarcula marismortui, J. Bacteriol. 183, 4149-4156.
    • (2001) J. Bacteriol. , vol.183 , pp. 4149-4156
    • Ichiki, H.1    Tanaka, Y.2    Mochizuki, K.3    Yoshimatsu, K.4    Sakurai, T.5    Fujiwara, T.6
  • 5
    • 0036550077 scopus 로고    scopus 로고
    • Nitric oxide in biological denitrification: Fe/Cu metalloenzyme and metal complex NOx redox chemistry
    • Wasser, I. M., de Vries, S., Moenne-Loccoz, P., Schroder, I., and Karlin, K. D. (2002) Nitric Oxide in Biological Denitrification: Fe/Cu Metalloenzyme and Metal Complex NOx Redox Chemistry, Chem. Rev. 102, 1201-1234.
    • (2002) Chem. Rev. , vol.102 , pp. 1201-1234
    • Wasser, I.M.1    De Vries, S.2    Moenne-Loccoz, P.3    Schroder, I.4    Karlin, K.D.5
  • 6
    • 0001076517 scopus 로고    scopus 로고
    • Dissimilatory nitrite and nitric oxide reductases
    • Averill. B. A. (1996) Dissimilatory Nitrite and Nitric Oxide Reductases, Chem. Rev. 96, 2951-2964.
    • (1996) Chem. Rev. , vol.96 , pp. 2951-2964
    • Averill, B.A.1
  • 7
    • 0033944864 scopus 로고    scopus 로고
    • Expression of AniA, the major anaerobically induced outer membrane protein of Neisseria gonorrhoeae, provides protection against killing by normal human sera
    • Cardinale, J. A., and Clark, V. L. (2000) Expression of AniA, the major anaerobically induced outer membrane protein of Neisseria gonorrhoeae, provides protection against killing by normal human sera, Infect. Immun. 68, 4368-4369.
    • (2000) Infect. Immun. , vol.68 , pp. 4368-4369
    • Cardinale, J.A.1    Clark, V.L.2
  • 8
    • 0026353602 scopus 로고
    • The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes
    • Godden, J. W., Turley, S., Teller, D. C., Adman, E. T., Liu, M. Y., Payne, W. J., and LeGall, J. (1991) The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes, Science 253, 438-442.
    • (1991) Science , vol.253 , pp. 438-442
    • Godden, J.W.1    Turley, S.2    Teller, D.C.3    Adman, E.T.4    Liu, M.Y.5    Payne, W.J.6    LeGall, J.7
  • 9
    • 0026701748 scopus 로고
    • Evidence that the type 2 copper centers are the site of nitrite reduction by Achromobacter cycloclastes nitrite reductase
    • Libby, E., and Averill, B. A. (1992) Evidence that the type 2 copper centers are the site of nitrite reduction by Achromobacter cycloclastes nitrite reductase, Biochem. Biophys. Res. Commun. 187, 1529-1535.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 1529-1535
    • Libby, E.1    Averill, B.A.2
  • 11
    • 0028298314 scopus 로고
    • X-ray structure and site-directed mutagenesis of a nitrite reductase from Alcaligenes faecalis S-6: Roles of two copper atoms in nitrite reduction
    • Kukimoto, M., Nishiyama, M., Murphy, M. E., Turley, S., Adman, E. T., Horinouchi, S., and Beppu, T. (1994) X-ray structure and site-directed mutagenesis of a nitrite reductase from Alcaligenes faecalis S-6: roles of two copper atoms in nitrite reduction, Biochemistry 33, 5246-5252.
    • (1994) Biochemistry , vol.33 , pp. 5246-5252
    • Kukimoto, M.1    Nishiyama, M.2    Murphy, M.E.3    Turley, S.4    Adman, E.T.5    Horinouchi, S.6    Beppu, T.7
  • 12
    • 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., Horinouchi, S., and Beppu, T. (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    Beppu, T.7
  • 13
    • 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, 13680-13683.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13680-13683
    • Kukimoto, M.1    Nishiyama, M.2    Tanokura, M.3    Adman, E.T.4    Horinouchi, S.5
  • 14
    • 0019498490 scopus 로고
    • A blue protein as an inactivating factor for nitrite reductase from Alcaligenes faecalis strain S-6
    • Kakutani, T., Watanabe, H., Arima, K., and Beppu, T. (1981) A blue protein as an inactivating factor for nitrite reductase from Alcaligenes faecalis strain S-6, J. Biochem. (Tokyo) 89, 463-472.
    • (1981) J. Biochem. (Tokyo) , vol.89 , pp. 463-472
    • Kakutani, T.1    Watanabe, H.2    Arima, K.3    Beppu, T.4
  • 15
    • 2442477353 scopus 로고    scopus 로고
    • Mapping of the binding site on pseudoazurin in the transient 152 kDa complex with nitrite reductase
    • Impagliazzo, A., and Ubbink, M. (2004) Mapping of the binding site on pseudoazurin in the transient 152 kDa complex with nitrite reductase, J. Am. Chem. Soc. 126, 5658-5659.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5658-5659
    • Impagliazzo, A.1    Ubbink, M.2
  • 16
    • 0032574685 scopus 로고    scopus 로고
    • Electronic structural information from Q-band ENDOR on the type 1 and type 2 copper liganding environment in wild-type and mutant forms of copper-containing nitrite reductase
    • Veselov, A., Olesen, K., Sienkiewicz, A., Shapleigh, J. P., and Scholes, C. P. (1998) Electronic structural information from Q-band ENDOR on the type 1 and type 2 copper liganding environment in wild-type and mutant forms of copper-containing nitrite reductase, Biochemistry 37, 6095-6105.
    • (1998) Biochemistry , vol.37 , pp. 6095-6105
    • Veselov, A.1    Olesen, K.2    Sienkiewicz, A.3    Shapleigh, J.P.4    Scholes, C.P.5
  • 17
    • 0037062623 scopus 로고    scopus 로고
    • Catalytic function and local proton structure at the type 2 copper of nitrite reductase: The correlation of enzymatic pH dependence, conserved residues, and proton hyperfine structure
    • Zhao, Y., Lukoyanov, D. A., Toropov, Y. V., Wu, K., Shapleigh, J. P., and Scholes, C. P. (2002) Catalytic function and local proton structure at the type 2 copper of nitrite reductase: the correlation of enzymatic pH dependence, conserved residues, and proton hyperfine structure, Biochemistry 41, 7464-7474.
    • (2002) Biochemistry , vol.41 , pp. 7464-7474
    • Zhao, Y.1    Lukoyanov, D.A.2    Toropov, Y.V.3    Wu, K.4    Shapleigh, J.P.5    Scholes, C.P.6
  • 19
    • 0035863096 scopus 로고    scopus 로고
    • Catalytic and spectroscopic analysis of blue copper-containing nitrite reductase mutants altered in the environment of the type 2 copper centre: Implications for substrate interaction
    • Prudêncio, M., Eady, R. R., and Sawers, G. (2001) Catalytic and spectroscopic analysis of blue copper-containing nitrite reductase mutants altered in the environment of the type 2 copper centre: implications for substrate interaction, Biochem. J. 353, 259-266.
    • (2001) Biochem. J. , vol.353 , pp. 259-266
    • Prudêncio, M.1    Eady, R.R.2    Sawers, G.3
  • 20
    • 0037220858 scopus 로고    scopus 로고
    • Characterization of two Cu-containing protein fragments obtained by limited proteolysis of Hyphomicrobium denitrificans A3151 nitrite reductase
    • Yamaguchi, K., Kobayashi, M., Kataoka, K., and Suzuki, S. (2003) Characterization of two Cu-containing protein fragments obtained by limited proteolysis of Hyphomicrobium denitrificans A3151 nitrite reductase, Biochem. Biophys. Res. Commun. 300, 36-40.
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 36-40
    • Yamaguchi, K.1    Kobayashi, M.2    Kataoka, K.3    Suzuki, S.4
  • 21
    • 0034604550 scopus 로고    scopus 로고
    • Catalytic roles for two water bridged residues (Asp-98 and His-255) in the active site of copper-containing nitrite reductase
    • Boulanger, M. J., Kukimoto, M., Nishiyama, M., Horinouchi, S., and Murphy, M. E. (2000) Catalytic roles for two water bridged residues (Asp-98 and His-255) in the active site of copper-containing nitrite reductase J. Biol. Chem. 275, 23957-23964.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23957-23964
    • Boulanger, M.J.1    Kukimoto, M.2    Nishiyama, M.3    Horinouchi, S.4    Murphy, M.E.5
  • 22
    • 0030658026 scopus 로고    scopus 로고
    • Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis, Mechanistic implications
    • Murphy, M. E., Turley, S., and Adman, E. T. (1997) Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications, J. Biol. Chem. 272, 28455-28460.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28455-28460
    • Murphy, M.E.1    Turley, S.2    Adman, E.T.3
  • 24
    • 0031786665 scopus 로고    scopus 로고
    • Type 1 Cu structure of blue nitrite reductase from Alcaligenes xylosoxidans GIFU 1051 at 2.05 Å resolution: Comparison of blue and green nitrite reductases
    • Inoue, T., Gotowda, M., Deligeer, Kataoka, K., Yamaguchi, K., Suzuki, S., Watanabe, H., Gohow, M., and Kai, Y. (1998) Type 1 Cu structure of blue nitrite reductase from Alcaligenes xylosoxidans GIFU 1051 at 2.05 Å resolution: Comparison of blue and green nitrite reductases, J. Biochem. (Tokyo) 124, 876-879.
    • (1998) J. Biochem. (Tokyo) , vol.124 , pp. 876-879
    • Inoue, T.1    Gotowda, M.2    Deligeer3    Kataoka, K.4    Yamaguchi, K.5    Suzuki, S.6    Watanabe, H.7    Gohow, M.8    Kai, Y.9
  • 25
    • 0032544483 scopus 로고    scopus 로고
    • X-ray structure of a blue-copper nitrite reductase in two crystal forms. The nature of the copper sites, mode of substrate binding and recognition by redox partner
    • Dodd, F. E., Van Beeumen, J., Eady, R. R., and Hasnain, S. S. (1998) X-ray structure of a blue-copper nitrite reductase in two crystal forms. The nature of the copper sites, mode of substrate binding and recognition by redox partner, J. Mol. Biol. 282, 369-382.
    • (1998) J. Mol. Biol. , vol.282 , pp. 369-382
    • Dodd, F.E.1    Van Beeumen, J.2    Eady, R.R.3    Hasnain, S.S.4
  • 26
    • 0028267847 scopus 로고
    • EPR and electron nuclear double resonance (ENDOR) studies show nitrite binding to the type 2 copper centers of the dissimilatory nitrite reductase of Alcaligenes xylosoxidans (NCIMB 11015)
    • Howes, B. D., Abraham, Z. H., Lowe, D. J., Bruser, T., Eady, R. R., and Smith, B. E. (1994) EPR and electron nuclear double resonance (ENDOR) studies show nitrite binding to the type 2 copper centers of the dissimilatory nitrite reductase of Alcaligenes xylosoxidans (NCIMB 11015), Biochemistry 33, 3171-3177.
    • (1994) Biochemistry , vol.33 , pp. 3171-3177
    • Howes, B.D.1    Abraham, Z.H.2    Lowe, D.J.3    Bruser, T.4    Eady, R.R.5    Smith, B.E.6
  • 27
    • 0035822630 scopus 로고    scopus 로고
    • Alternate substrate binding modes to two mutant (D98N and H255N) forms of nitrite reductase from Alcaligenes faecalis S-6: Structural model of a transient catalytic intermediate
    • Boulanger, M. J., and Murphy, M. E. (2001) Alternate substrate binding modes to two mutant (D98N and H255N) forms of nitrite reductase from Alcaligenes faecalis S-6: Structural model of a transient catalytic intermediate, Biochemistry 40, 9132-9141.
    • (2001) Biochemistry , vol.40 , pp. 9132-9141
    • Boulanger, M.J.1    Murphy, M.E.2
  • 28
    • 0037304281 scopus 로고    scopus 로고
    • Directing the mode of nitrite binding to a copper-containing nitrite reductase from Alcaligenes faecalis S-6: Characterization of an active site isoleucine
    • Boulanger, M. J., and Murphy, M. E. P. (2003) Directing the mode of nitrite binding to a copper-containing nitrite reductase from Alcaligenes faecalis S-6: Characterization of an active site isoleucine, Protein Sci. 12, 248-256.
    • (2003) Protein Sci. , vol.12 , pp. 248-256
    • Boulanger, M.J.1    Murphy, M.E.P.2
  • 29
    • 0034097583 scopus 로고    scopus 로고
    • Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase
    • Kataoka, K., Furusawa, H., Takagi, K., Yamaguchi, K., and Suzuki, S. (2000) Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase, J. Biochem. (Tokyo) 127, 345-350.
    • (2000) J. Biochem. (Tokyo) , vol.127 , pp. 345-350
    • Kataoka, K.1    Furusawa, H.2    Takagi, K.3    Yamaguchi, K.4    Suzuki, S.5
  • 30
    • 0034319668 scopus 로고    scopus 로고
    • Carbons monoxide binding to copper-containing nitrite reductase from Alcaligenes faecalis
    • Zhang, H. M., Boulanger, M. J., Mauk, A. G., and Murphy, M. E. P. (2000) Carbons monoxide binding to copper-containing nitrite reductase from Alcaligenes faecalis, J. Phys. Chem. B 104, 10738-10742.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 10738-10742
    • Zhang, H.M.1    Boulanger, M.J.2    Mauk, A.G.3    Murphy, M.E.P.4
  • 32
    • 0032839514 scopus 로고    scopus 로고
    • The pH-dependent changes of intramolecular electron transfer on copper-containing nitrite reductase
    • Kobayashi, K., Tagawa, S., Deligeer, and Suzuki, S. (1999) The pH-dependent changes of intramolecular electron transfer on copper-containing nitrite reductase, J. Biochem. (Tokyo) 126,408-412.
    • (1999) J. Biochem. (Tokyo) , vol.126 , pp. 408-412
    • Kobayashi, K.1    Tagawa, S.2    Deligeer3    Suzuki, S.4
  • 33
    • 0027229994 scopus 로고
    • Cloning and characterization of a nitrite reductase gene from Alcaligenes faecalis and its expression in Escherichia coli
    • Nishiyama, M., Suzuki, J., Kukimoto, M., Ohnuki, T., Horinouchi, S., and Beppu, T. (1993) Cloning and characterization of a nitrite reductase gene from Alcaligenes faecalis and its expression in Escherichia coli, J. Gen. Microbiol. 139, 725-733.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 725-733
    • Nishiyama, M.1    Suzuki, J.2    Kukimoto, M.3    Ohnuki, T.4    Horinouchi, S.5    Beppu, T.6
  • 35
    • 0019457194 scopus 로고
    • Purification and properties of a copper-containing nitrite reductase from a denitrifying bacterium, Alcaligenes faecalis strain S-6
    • Kakutani, T., Watanabe, H., Arima, K., and Beppu, T. (1981) Purification and properties of a copper-containing nitrite reductase from a denitrifying bacterium, Alcaligenes faecalis strain S-6, J. Biochem. (Tokyo) 89, 453-461.
    • (1981) J. Biochem. (Tokyo) , vol.89 , pp. 453-461
    • Kakutani, T.1    Watanabe, H.2    Arima, K.3    Beppu, T.4
  • 36
    • 0028945240 scopus 로고
    • A quantitative test for copper using bicinchoninic acid
    • Brenner, A. J., and Harris, E. D. (1995) A quantitative test for copper using bicinchoninic acid, Anal. Biochem. 226, 80-84 [erratum (1995) Anal. Biochem. 230, 36O].
    • (1995) Anal. Biochem. , vol.226 , pp. 80-84
    • Brenner, A.J.1    Harris, E.D.2
  • 37
    • 0028945240 scopus 로고
    • Erratum
    • Brenner, A. J., and Harris, E. D. (1995) A quantitative test for copper using bicinchoninic acid, Anal. Biochem. 226, 80-84 [erratum (1995) Anal. Biochem. 230, 36O].
    • (1995) Anal. Biochem. , vol.230
  • 39
    • 0031028099 scopus 로고    scopus 로고
    • Purification and initial kinetic and spectroscopic characterization of NO reductase from Paracoccus denitrificans
    • Girsch, P., and de Vries, S. (1997) Purification and initial kinetic and spectroscopic characterization of NO reductase from Paracoccus denitrificans, Biochim. Biophys. Acta 1318, 202-216.
    • (1997) Biochim. Biophys. Acta , vol.1318 , pp. 202-216
    • Girsch, P.1    De Vries, S.2
  • 40
    • 0000497698 scopus 로고
    • Reactivity of pseudoazurin from Achromobacter cycloclastes with inorganic redox partners and related NMR and electrochemical studies
    • Dennison, C., Kohzuma, T., McFarlane, W., Suzuki, S., and Sykes, A. G. (1994) Reactivity of pseudoazurin from Achromobacter cycloclastes with inorganic redox partners and related NMR and electrochemical studies, Inorg. Chem. 33, 3299-3305.
    • (1994) Inorg. Chem. , vol.33 , pp. 3299-3305
    • Dennison, C.1    Kohzuma, T.2    McFarlane, W.3    Suzuki, S.4    Sykes, A.G.5
  • 41
    • 0037039418 scopus 로고    scopus 로고
    • Effect of histidine 6 protonation on the active site structure and electron-transfer capabilities of pseudoazurin from Achromobacter cycloclastes
    • Sato, K., and Dennison, C. (2002) Effect of histidine 6 protonation on the active site structure and electron-transfer capabilities of pseudoazurin from Achromobacter cycloclastes, Biochemistry 41, 120-130.
    • (2002) Biochemistry , vol.41 , pp. 120-130
    • Sato, K.1    Dennison, C.2
  • 42
    • 77956997457 scopus 로고
    • Determination of nitrate and nitrite
    • Nicholas, D. J. D., and Nason, A. (1957) Determination of nitrate and nitrite, Methods Enzymol. 3, 981-984.
    • (1957) Methods Enzymol. , vol.3 , pp. 981-984
    • Nicholas, D.J.D.1    Nason, A.2
  • 45
    • 0017343370 scopus 로고
    • Energy Conservation in chemotrophic anaerobic bacteria
    • Thauer, R. K., Jungermann, K., and Decker, K. (1977) Energy Conservation in chemotrophic anaerobic bacteria, Bacterial. Rev. 41, 100-180.
    • (1977) Bacterial. Rev. , vol.41 , pp. 100-180
    • Thauer, R.K.1    Jungermann, K.2    Decker, K.3
  • 46
    • 0023645836 scopus 로고
    • The reaction of nitric oxide with copper proteins and the photodissociation of copper-NO complexes
    • Gorren, A. C., de Boer, E., and Wever, R. (1987) The reaction of nitric oxide with copper proteins and the photodissociation of copper-NO complexes, Biochim. Biophys. Acta 916, 38-47.
    • (1987) Biochim. Biophys. Acta , vol.916 , pp. 38-47
    • Gorren, A.C.1    De Boer, E.2    Wever, R.3
  • 47
    • 0020064009 scopus 로고
    • Denitrification
    • Knowles, R. (1982) Denitrification, Microbiol. Rev. 46, 43-70.
    • (1982) Microbiol. Rev. , vol.46 , pp. 43-70
    • Knowles, R.1
  • 49
    • 0031033309 scopus 로고    scopus 로고
    • Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases
    • Xu, F. (1997) Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases, J. Biol. Chem. 272, 924-928.
    • (1997) J. Biol. Chem. , vol.272 , pp. 924-928
    • Xu, F.1
  • 51
    • 0025768943 scopus 로고
    • Evidence for a NO-rebound mechanism for production of N2O from nitrite by the copper-containing nitrite reductase from Achromobacter cycloclastes
    • Jackson, M. A., Tiedje, J. M., and Averill, B. A. (1991) Evidence for a NO-rebound mechanism for production of N2O from nitrite by the copper-containing nitrite reductase from Achromobacter cycloclastes, FEBS Lett. 291, 41-44.
    • (1991) FEBS Lett. , vol.291 , pp. 41-44
    • Jackson, M.A.1    Tiedje, J.M.2    Averill, B.A.3
  • 52
    • 0025287522 scopus 로고
    • Steady-state nitric oxide concentrations during denitrification
    • Goretski, J., Zafiriou, O. C., and Hollocher, T. C. (1990) Steady-state nitric oxide concentrations during denitrification, J. Biol. Chem. 265, 11535-11538.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11535-11538
    • Goretski, J.1    Zafiriou, O.C.2    Hollocher, T.C.3
  • 53
    • 50549159930 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products
    • Cleland, W. W. (1963) The kinetics of enzyme-catalyzed reactions with two or more substrates or products, Biochim. Biophys. Acta 67, 104-137.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 54
    • 0001678195 scopus 로고    scopus 로고
    • Interpreting the catalytic voltammetry of electroactive enzymes adsorbed on electrodes
    • Heering, H. A., Hirst, J., and Armstrong, F. A. (1998) Interpreting the catalytic voltammetry of electroactive enzymes adsorbed on electrodes, J. Phys. Chem. B 102, 6889-6902.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 6889-6902
    • Heering, H.A.1    Hirst, J.2    Armstrong, F.A.3
  • 55
    • 0346366817 scopus 로고    scopus 로고
    • Redox characteristics of the tungsten DMSO reductase of Rhodobacter capsulatus
    • Hagedoorn, P. L., Hagen, W. R., Stewart, L. J., Docrat, A., Bailey, S., and Garner, C. D. (2003) Redox characteristics of the tungsten DMSO reductase of Rhodobacter capsulatus, FEBS Lett. 555, 606-610.
    • (2003) FEBS Lett. , vol.555 , pp. 606-610
    • Hagedoorn, P.L.1    Hagen, W.R.2    Stewart, L.J.3    Docrat, A.4    Bailey, S.5    Garner, C.D.6
  • 57
    • 0026583356 scopus 로고
    • Diode-like behaviour of a mitochondrial electron-transport enzyme
    • Sucheta, A., Ackrell, B. A., Cochran, B., and Armstrong, F. A. (1992) Diode-like behaviour of a mitochondrial electron-transport enzyme, Nature 356, 361-362.
    • (1992) Nature , vol.356 , pp. 361-362
    • Sucheta, A.1    Ackrell, B.A.2    Cochran, B.3    Armstrong, F.A.4
  • 58
    • 0030817887 scopus 로고    scopus 로고
    • Global observation of hydrogen/deuterium isotope effects on bidirectional catalytic electron transport in an enzyme: Direct measurement by protein-film voltammetry
    • Hirst, J., Ackrell, B. A. C., and Armstrong, F. A. (1997) Global observation of hydrogen/deuterium isotope effects on bidirectional catalytic electron transport in an enzyme: Direct measurement by protein-film voltammetry, J. Am. Chem. Soc. 119, 7434-7439.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 7434-7439
    • Hirst, J.1    Ackrell, B.A.C.2    Armstrong, F.A.3
  • 59
    • 15844392907 scopus 로고    scopus 로고
    • Electrocatalytic voltammetry of succinate dehydrogenase: Direct quantification of the catalytic properties of a complex electron-transport enzyme
    • Hirst, J., Sucheta, A., Ackrell, B. A. C., and Armstrong, F. A. (1996) Electrocatalytic voltammetry of succinate dehydrogenase: Direct quantification of the catalytic properties of a complex electron-transport enzyme, J. Am. Chem. Soc. 118, 5031-5038.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 5031-5038
    • Hirst, J.1    Sucheta, A.2    Ackrell, B.A.C.3    Armstrong, F.A.4
  • 60
    • 0032574836 scopus 로고    scopus 로고
    • Spectroscopic, kinetic, and electrochemical characterization of heterologously expressed wild-type and mutant forms of copper-containing nitrite reductase from Rhodobacter sphaeroides 2.4.3
    • Olesen, K., Veselov, A., Zhao, Y., Wang, Y., Danner, B., Scholes, C. P., and Shapleigh, J. P. (1998) Spectroscopic, kinetic, and electrochemical characterization of heterologously expressed wild-type and mutant forms of copper-containing nitrite reductase from Rhodobacter sphaeroides 2.4.3, Biochemistry 37, 6086-6094.
    • (1998) Biochemistry , vol.37 , pp. 6086-6094
    • Olesen, K.1    Veselov, A.2    Zhao, Y.3    Wang, Y.4    Danner, B.5    Scholes, C.P.6    Shapleigh, J.P.7
  • 62
    • 0000679937 scopus 로고
    • Preparation of crystalline Pseudomonas cytochrome c-551 and its general properties
    • Horio, T., Higashi, T., Sasagawa, M., Kusai, K., Nakai, M., and Okunuki, K. (1960) Preparation of crystalline Pseudomonas cytochrome c-551 and its general properties, Biochem. J. 77, 194-201.
    • (1960) Biochem. J. , vol.77 , pp. 194-201
    • Horio, T.1    Higashi, T.2    Sasagawa, M.3    Kusai, K.4    Nakai, M.5    Okunuki, K.6
  • 63
    • 0034846778 scopus 로고    scopus 로고
    • Kinetics of inter- and intramolecular electron transfer of Pseudomonas nautica cytochrome cd1 nitrite reductase: Regulation of the NO-bound end product
    • Lopes, H., Besson, S., Moura, I., and Moura, J. J. (2001) Kinetics of inter- and intramolecular electron transfer of Pseudomonas nautica cytochrome cd1 nitrite reductase: regulation of the NO-bound end product, J. Biol. Inorg. Chem. 6, 55-62.
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 55-62
    • Lopes, H.1    Besson, S.2    Moura, I.3    Moura, J.J.4
  • 64
    • 0027340210 scopus 로고
    • 1-type nitrite reductase from, and the absence of a copper-type nitrite reductase from, the aerobic denitrifier Thiosphaera pantotropha; the role of pseudoazurin as an electron donor
    • 1-type nitrite reductase from, and the absence of a copper-type nitrite reductase from, the aerobic denitrifier Thiosphaera pantotropha; the role of pseudoazurin as an electron donor, Eur. J. Biochem. 212, 377-385.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 377-385
    • Moir, J.W.1    Baratta, D.2    Richardson, D.J.3    Ferguson, S.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.