메뉴 건너뛰기




Volumn 155, Issue 2, 2014, Pages 123-135

Structural insights into the function of a thermostable copper-containing nitrite reductase

Author keywords

Copper; Enzyme; Metallo; Metals; Methods; Oxidation Reduction; Thermostable enzyme; X ray Crystallography

Indexed keywords

CHLORIDE; COPPER; COPPER CONTAINING NITRITE REDUCTASE; FORMIC ACID; NITRITE; NITRITE REDUCTASE; PROTON; SOLVENT; UNCLASSIFIED DRUG; WATER;

EID: 84893249131     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvt107     Document Type: Article
Times cited : (20)

References (56)
  • 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
    • 38349190507 scopus 로고    scopus 로고
    • An Earth-system perspective of the global nitrogen cycle
    • Gruber, N. and Galloway, J.N. (2008) An Earth-system perspective of the global nitrogen cycle. Nature 451, 293-296
    • (2008) Nature , vol.451 , pp. 293-296
    • Gruber, N.1    Galloway, J.N.2
  • 4
    • 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. Coordination Chem. Rev. 190-192, 245-265
    • (1999) Coordination Chem. Rev. , vol.190-192 , pp. 245-265
    • Suzuki, S.1    Kataoka, K.2    Yamaguchi, K.3    Inoue, T.4    Kai, Y.5
  • 7
    • 84879967534 scopus 로고    scopus 로고
    • Structural and mechanistic insights into the electron flow through protein for cytochrome c-tethering copper nitrite reductase
    • Tsuda, A., Ishikawa, R., Koteishi, H., Tange, K., Fukuda, Y., Kobayashi, K., Inoue, T., and Nojiri, M. (2013) Structural and mechanistic insights into the electron flow through protein for cytochrome c-tethering copper nitrite reductase. J. Biochem. 154, 51-60
    • (2013) J. Biochem. , vol.154 , pp. 51-60
    • Tsuda, A.1    Ishikawa, R.2    Koteishi, H.3    Tange, K.4    Fukuda, Y.5    Kobayashi, K.6    Inoue, T.7    Nojiri, M.8
  • 8
    • 70449116515 scopus 로고    scopus 로고
    • Structural basis of inter-protein electron transfer for nitrite reduction in denitrification
    • Nojiri, M., Koteishi, H., Nakagami, T., Kobayashi, K., Inoue, T., Yamaguchi, K., and Suzuki, S. (2009) Structural basis of inter-protein electron transfer for nitrite reduction in denitrification. Nature 462, 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
  • 9
    • 68949189201 scopus 로고    scopus 로고
    • Cytochrome c551 is a mediator of electron transfer between copper-containing nitrite reductase and azurin in a denitrifying bacterium Achromobacter xylosoxidans
    • Koteishi, H., Nojiri, M., Nakagami, T., Yamaguchi, K., and Suzuki, S. (2009) Cytochrome c551 is a mediator of electron transfer between copper-containing nitrite reductase and azurin in a denitrifying bacterium, Achromobacter xylosoxidans. Bull. Chem. Soc. Jpn. 82, 1003-1005
    • (2009) Bull. Chem. Soc. Jpn. , vol.82 , pp. 1003-1005
    • Koteishi, H.1    Nojiri, M.2    Nakagami, T.3    Yamaguchi, K.4    Suzuki, S.5
  • 10
    • 37549050579 scopus 로고    scopus 로고
    • Conformation of pseudoazurin in the 152 kDa electron transfer complex with nitrite reductase determined by paramagnetic NMR
    • Vlasie, M.D., Fernandez-Busnadiego, R., Prudencio, M., and Ubbink, M. (2008) Conformation of pseudoazurin in the 152 kDa electron transfer complex with nitrite reductase determined by paramagnetic NMR. J. Mol. Biol. 375, 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
  • 11
    • 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. Prot. Engin. 8, 153-158
    • (1995) Prot. Engin. , 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
  • 12
    • 0030920834 scopus 로고    scopus 로고
    • PH-dependence for binding a single nitrite ion to each type-2 copper centre in the copper-containing nitrite reductase of Alcaligenes xylosoxidans
    • Abraham, Z.H.L., Smith, B.E., Howes, B.D., Lowe, D.J., and Eady, R.R. (1997) pH-dependence for binding a single nitrite ion to each type-2 copper centre in the copper-containing nitrite reductase of Alcaligenes xylosoxidans. Biochem. J. 324, 511-516
    • (1997) Biochem. J. , vol.324 , pp. 511-516
    • Abraham, Z.H.L.1    Smith, B.E.2    Howes, B.D.3    Lowe, D.J.4    Eady, R.R.5
  • 13
    • 0030658026 scopus 로고    scopus 로고
    • Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis
    • Murphy, M.E.P., Turley, S., and Adman, E.T. (1997) Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. J. Biol. Chem. 272, 28455-28460
    • (1997) J. Biol. Chem. , vol.272 , pp. 28455-28460
    • Murphy, M.E.P.1    Turley, S.2    Adman, E.T.3
  • 14
    • 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. 127, 345-350
    • (2000) J. Biochem. , vol.127 , pp. 345-350
    • Kataoka, K.1    Furusawa, H.2    Takagi, K.3    Yamaguchi, K.4    Suzuki, S.5
  • 15
    • 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
  • 16
    • 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.P. (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.P.2
  • 17
    • 2442604589 scopus 로고    scopus 로고
    • Side-on copper-nitrosyl coordination by nitrite reductase
    • Tocheva, E.I., Rosell, F.I., Mauk, A.G., and Murphy, M.E. (2004) Side-on copper-nitrosyl coordination by nitrite reductase. Science 304, 867-870
    • (2004) Science , vol.304 , pp. 867-870
    • Tocheva, E.I.1    Rosell, F.I.2    Mauk, A.G.3    Murphy, M.E.4
  • 18
    • 24744467360 scopus 로고    scopus 로고
    • Atomic resolution structures of resting-state, substrate-and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism
    • Antonyuk, S.V., Strange, R.W., Sawers, G., Eady, R.R., and Hasnain, S.S. (2005) Atomic resolution structures of resting-state, substrate-and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism. Proc. Natl Acad. Sci. USA. 102, 12041-12046
    • (2005) Proc. Natl Acad. Sci. USA. , vol.102 , pp. 12041-12046
    • Antonyuk, S.V.1    Strange, R.W.2    Sawers, G.3    Eady, R.R.4    Hasnain, S.S.5
  • 19
    • 70350025521 scopus 로고    scopus 로고
    • Demonstration of proton-coupled electron transfer in the copper-containing nitrite reductases
    • Brenner, S., Heyes, D.J., Hay, S., Hough, M.A., Eady, R.R., Hasnain, S.S., and Scrutton, N.S. (2009) Demonstration of proton-coupled electron transfer in the copper-containing nitrite reductases. J. Biol. Chem. 284, 25973-25983
    • (2009) J. Biol. Chem. , vol.284 , pp. 25973-25983
    • Brenner, S.1    Heyes, D.J.2    Hay, S.3    Hough, M.A.4    Eady, R.R.5    Hasnain, S.S.6    Scrutton, N.S.7
  • 21
    • 49749112308 scopus 로고    scopus 로고
    • Phylogenetic analysis of nitrite, nitric oxide, and nitrous oxide respiratory enzymes reveal a complex evolutionary history for denitrification
    • Jones, C.M., Stres, B., Rosenquist, M., and Hallin, S. (2008) Phylogenetic analysis of nitrite, nitric oxide, and nitrous oxide respiratory enzymes reveal a complex evolutionary history for denitrification. Mol. Biol. Evol. 25, 1955-1966
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 1955-1966
    • Jones, C.M.1    Stres, B.2    Rosenquist, M.3    Hallin, S.4
  • 22
    • 65549128998 scopus 로고    scopus 로고
    • Eukaryotic nirK genes encoding copper-containing nitrite reductase: Originating from the protomitochondrion?
    • Kim, S.W., Fushinobu, S., Zhou, S., Wakagi, T., and Shoun, H. (2009) Eukaryotic nirK genes encoding copper-containing nitrite reductase: originating from the protomitochondrion? Appl. Environ. Microbiol. 75, 2652-2658
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 2652-2658
    • Kim, S.W.1    Fushinobu, S.2    Zhou, S.3    Wakagi, T.4    Shoun, H.5
  • 23
    • 84875883028 scopus 로고    scopus 로고
    • Structures of protein-protein complexes involved in electron transfer
    • Antonyuk, S.V., Han, C., Eady, R.R., and Hasnain, S.S. (2013) Structures of protein-protein complexes involved in electron transfer. Nature 496, 123-126
    • (2013) Nature , vol.496 , pp. 123-126
    • Antonyuk, S.V.1    Han, C.2    Eady, R.R.3    Hasnain, S.S.4
  • 25
    • 25444443909 scopus 로고    scopus 로고
    • Geobacillus thermoleovorans subsp. Stromboliensis subsp. Nov., Isolated from the geothermal volcanic environment
    • Romano, I., Poli, A., Lama, L., Gambacorta, A., and Nicolaus, B. (2005) Geobacillus thermoleovorans subsp. stromboliensis subsp. nov., isolated from the geothermal volcanic environment. J. Gen. Appl. Microbiol. 51, 183-189
    • (2005) J. Gen. Appl. Microbiol. , vol.51 , pp. 183-189
    • Romano, I.1    Poli, A.2    Lama, L.3    Gambacorta, A.4    Nicolaus, B.5
  • 26
    • 67649212273 scopus 로고    scopus 로고
    • Cultivation characteristics of denitrification by thermophilic Geobacillus sp. Strain TDN01
    • Mishima, M., Iwata, K., Nara, K., Matsui, T., Shigeno, T., and Omori, T. (2009) Cultivation characteristics of denitrification by thermophilic Geobacillus sp. strain TDN01. J. Gen. Appl. Microbiol. 55, 81-86
    • (2009) J. Gen. Appl. Microbiol. , vol.55 , pp. 81-86
    • Mishima, M.1    Iwata, K.2    Nara, K.3    Matsui, T.4    Shigeno, T.5    Omori, T.6
  • 27
    • 79958107996 scopus 로고    scopus 로고
    • Cloning, expression, purification, crystallization and preliminary X-ray crystallographic study of GK0767, the copper-containing nitrite reductase from Geobacillus kaustophilus
    • Fukuda, Y., Tamada, T., Takami, H., Suzuki, S., Inoue, T., and Nojiri, M. (2011) Cloning, expression, purification, crystallization and preliminary X-ray crystallographic study of GK0767, the copper-containing nitrite reductase from Geobacillus kaustophilus. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67, 692-695
    • (2011) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.67 , pp. 692-695
    • Fukuda, Y.1    Tamada, T.2    Takami, H.3    Suzuki, S.4    Inoue, T.5    Nojiri, M.6
  • 30
    • 34248385250 scopus 로고    scopus 로고
    • Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir
    • Feng, L., Wang, W., Cheng, J., Ren, Y., Zhao, G., Gao, C., Tang, Y., Liu, X., Han, W., Peng, X., Liu, R., and Wang, L. (2007) Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir. Proc. Natl Acad. Sci. USA. 104, 5602-5607
    • (2007) Proc. Natl Acad. Sci. USA. , vol.104 , pp. 5602-5607
    • Feng, L.1    Wang, W.2    Cheng, J.3    Ren, Y.4    Zhao, G.5    Gao, C.6    Tang, Y.7    Liu, X.8    Han, W.9    Peng, X.10    Liu, R.11    Wang, L.12
  • 31
    • 41249101880 scopus 로고    scopus 로고
    • Crystallography with online optical and X-ray absorption spectroscopies demonstrates an ordered mechanism in copper nitrite reductase
    • Hough, M.A., Antonyuk, S.V., Strange, R.W., Eady, R.R., and Hasnain, S.S. (2008) Crystallography with online optical and X-ray absorption spectroscopies demonstrates an ordered mechanism in copper nitrite reductase. J. Mol. Biol. 378, 353-361
    • (2008) J. Mol. Biol. , vol.378 , pp. 353-361
    • Hough, M.A.1    Antonyuk, S.V.2    Strange, R.W.3    Eady, R.R.4    Hasnain, S.S.5
  • 32
    • 20444381694 scopus 로고    scopus 로고
    • High resolution structural studies of mutants provide insights into catalysis and electron transfer processes in copper nitrite reductase
    • Hough, M.A., Ellis, M.J., Antonyuk, S., Strange, R.W., Sawers, G., Eady, R.R., and Samar Hasnain, S. (2005) High resolution structural studies of mutants provide insights into catalysis and electron transfer processes in copper nitrite reductase. J. Mol. Biol. 350, 300-309
    • (2005) J. Mol. Biol. , vol.350 , pp. 300-309
    • Hough, M.A.1    Ellis, M.J.2    Antonyuk, S.3    Strange, R.W.4    Sawers, G.5    Eady, R.R.6    Samar Hasnain, S.7
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A. and Teplyakov, A. (1997) MOLREP: an automated program for molecular replacement. J. Appl. Cryst. 30, 1022-1025
    • (1997) J. Appl. Cryst. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 38
    • 0000243829 scopus 로고
    • PROCHECK-a program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1993) PROCHECK-a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 40
    • 85022468790 scopus 로고
    • Crystal structure and electron spin echo envelope modulation study of [Cu(II)(TEPA)(NO2)]PF6 (TEPA 14 tris[2-(2-pyridyl)ethyl]amine): A model for the purported structure of the nitrite derivative of hemocyanin
    • Jiang, F., Conry, R.R., Bubacco, L., Tyeklar, Z., Jacobson, R.R., Karlin, K.D., and Peisach, J. (1993) Crystal structure and electron spin echo envelope modulation study of [Cu(II)(TEPA)(NO2)]PF6 (TEPA 14 tris[2-(2-pyridyl)ethyl] amine): a model for the purported structure of the nitrite derivative of hemocyanin. J. Am. Chem. Soc. 115, 2093-2102
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 2093-2102
    • Jiang, F.1    Conry, R.R.2    Bubacco, L.3    Tyeklar, Z.4    Jacobson, R.R.5    Karlin, K.D.6    Peisach, J.7
  • 41
    • 0000263553 scopus 로고
    • Molecular structure of nitro-and nitrito-copper complexes as reaction intermediates in electrochemical reduction of nitrite to dinitrogen oxide
    • Komeda, N., Nagao, H., Kushi, Y., Adachi, G.-y., Suzuki, M., Uehara, A., and Tanaka, K. (1995) Molecular structure of nitro-and nitrito-copper complexes as reaction intermediates in electrochemical reduction of nitrite to dinitrogen oxide. Bull. Chem. Soc. Jpn. 68, 581-589
    • (1995) Bull. Chem. Soc. Jpn. , vol.68 , pp. 581-589
    • Komeda, N.1    Nagao, H.2    Kushi, Y.3    Adachi, G.-Y.4    Suzuki, M.5    Uehara, A.6    Tanaka, K.7
  • 42
    • 0036306042 scopus 로고    scopus 로고
    • Crystal structure of the soluble domain of the major anaerobically induced outer membrane protein (AniA) from pathogenic Neisseria: A new class of copper-containing nitrite reductases
    • Boulanger, M.J. and Murphy, M.E. (2002) Crystal structure of the soluble domain of the major anaerobically induced outer membrane protein (AniA) from pathogenic Neisseria: a new class of copper-containing nitrite reductases. J. Mol. Biol. 315, 1111-1127
    • (2002) J. Mol. Biol. , vol.315 , pp. 1111-1127
    • Boulanger, M.J.1    Murphy, M.E.2
  • 43
  • 44
    • 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., Beeumen, J.V., 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    Beeumen, J.V.2    Eady, R.R.3    Hasnain, S.S.4
  • 45
    • 11144298974 scopus 로고    scopus 로고
    • Insights into redox partner interactions and substrate binding in nitrite reductase from Alcaligenes xylosoxidans: Crystal structures of the Trp138His and His313Gln mutants
    • Barrett, M.L., Harris, R.L., Antonyuk, S., Hough, M.A., Ellis, M.J., Sawers, G., Eady, R.R., and Hasnain, S.S. (2004) Insights into redox partner interactions and substrate binding in nitrite reductase from Alcaligenes xylosoxidans: crystal structures of the Trp138His and His313Gln mutants. Biochemistry 43, 16311-16319
    • (2004) Biochemistry , vol.43 , pp. 16311-16319
    • Barrett, M.L.1    Harris, R.L.2    Antonyuk, S.3    Hough, M.A.4    Ellis, M.J.5    Sawers, G.6    Eady, R.R.7    Hasnain, S.S.8
  • 46
    • 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. (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.2
  • 47
    • 42049123859 scopus 로고    scopus 로고
    • Conserved active site residues limit inhibition of a copper-containing nitrite reductase by small molecules
    • Tocheva, E.I., Eltis, L.D., and Murphy, M.E.P. (2008) Conserved active site residues limit inhibition of a copper-containing nitrite reductase by small molecules. Biochemistry 47, 4452-4460
    • (2008) Biochemistry , vol.47 , pp. 4452-4460
    • Tocheva, E.I.1    Eltis, L.D.2    Murphy, M.E.P.3
  • 48
    • 73249140826 scopus 로고    scopus 로고
    • The side-on copper I) nitrosyl geometry in copper nitrite reductase is due to steric interactions with isoleucine-257
    • Merkle, A.C. and Lehnert, N. (2009) The side-on copper(I) nitrosyl geometry in copper nitrite reductase is due to steric interactions with isoleucine-257. Inorg. Chem. 48, 11504-11506
    • (2009) Inorg. Chem. , vol.48 , pp. 11504-11506
    • Merkle, A.C.1    Lehnert, N.2
  • 49
    • 0037466312 scopus 로고    scopus 로고
    • Atomic resolution structures of native copper nitrite reductase from Alcaligenes xylosoxidans and the active site mutant Asp92Glu
    • Ellis, M.J., Dodd, F.E., Sawers, G., Eady, R.R., and Hasnain, S.S. (2003) Atomic resolution structures of native copper nitrite reductase from Alcaligenes xylosoxidans and the active site mutant Asp92Glu. J. Mol. Biol. 328, 429-438
    • (2003) J. Mol. Biol. , vol.328 , pp. 429-438
    • Ellis, M.J.1    Dodd, F.E.2    Sawers, G.3    Eady, R.R.4    Hasnain, S.S.5
  • 50
    • 58149171908 scopus 로고    scopus 로고
    • Identification of the proton channel to the active site type 2 Cu center of nitrite reductase: Structural and enzymatic properties of the His254Phe and Asn90Ser mutants
    • Hough, M.A., Eady, R.R., and Hasnain, S.S. (2008) Identification of the proton channel to the active site type 2 Cu center of nitrite reductase: structural and enzymatic properties of the His254Phe and Asn90Ser mutants. Biochemistry 47, 13547-13553
    • (2008) Biochemistry , vol.47 , pp. 13547-13553
    • Hough, M.A.1    Eady, R.R.2    Hasnain, S.S.3
  • 52
    • 84863476935 scopus 로고    scopus 로고
    • Protonation-state determination in proteins using high-resolution X-ray crystallography: Effects of resolution and completeness
    • Fisher, S.J., Blakeley, M.P., Cianci, M., McSweeney, S., and Helliwell, J.R. (2012) Protonation-state determination in proteins using high-resolution X-ray crystallography: effects of resolution and completeness. Acta Crystallogr. D Biol. Crystallogr. 68, 800-809
    • (2012) Acta Crystallogr. D Biol. Crystallogr. , vol.68 , pp. 800-809
    • Fisher, S.J.1    Blakeley, M.P.2    Cianci, M.3    McSweeney, S.4    Helliwell, J.R.5
  • 54
    • 8444244797 scopus 로고    scopus 로고
    • Role of weak interactions in thermal stability of proteins
    • Ibrahim, B.S. and Pattabhi, V. (2004) Role of weak interactions in thermal stability of proteins. Biochem. Biophys. Res. Commun. 325, 1082-1089
    • (2004) Biochem. Biophys. Res. Commun. , vol.325 , pp. 1082-1089
    • Ibrahim, B.S.1    Pattabhi, V.2
  • 55
    • 33748329585 scopus 로고    scopus 로고
    • Isolation and characterization of a novel thermophilic Bacillus strain degrading long-chain n-alkanes
    • Wang, L., Tang, Y., Wang, S., Liu, R.L., Liu, M.Z., Zhang, Y., Liang, F.L., and Feng, L. (2006) Isolation and characterization of a novel thermophilic Bacillus strain degrading long-chain n-alkanes. Extremophiles 10, 347-356
    • (2006) Extremophiles , vol.10 , pp. 347-356
    • Wang, L.1    Tang, Y.2    Wang, S.3    Liu, R.L.4    Liu, M.Z.5    Zhang, Y.6    Liang, F.L.7    Feng, L.8
  • 56
    • 34249705142 scopus 로고    scopus 로고
    • Synthesis and spectroscopic characterization of copper(II)-nitrito complexes with hydrotris(pyrazolyl)-borate and related coligands
    • Lehnert, N., Cornelissen, U., Neese, F., Ono, T., Noguchi, Y., Okamoto, K.-i., and Fujisawa, K. (2007) Synthesis and spectroscopic characterization of copper(II)-nitrito complexes with hydrotris(pyrazolyl)-borate and related coligands. Inorg. Chem. 46, 3916-3933
    • (2007) Inorg. Chem. , vol.46 , pp. 3916-3933
    • Lehnert, N.1    Cornelissen, U.2    Neese, F.3    Ono, T.4    Noguchi, Y.5    Okamoto, K.-I.6    Fujisawa, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.