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Volumn 378, Issue 2, 2008, Pages 353-361

Crystallography with Online Optical and X-ray Absorption Spectroscopies Demonstrates an Ordered Mechanism in Copper Nitrite Reductase

Author keywords

electron gating; nitrite reductase; ordered mechanism; radiation damage; XAS

Indexed keywords

COPPER; COPPER NIRITE REDUCTASE; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

EID: 41249101880     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.01.097     Document Type: Article
Times cited : (79)

References (39)
  • 1
    • 0037059062 scopus 로고    scopus 로고
    • Catalysis at a dinuclear [CuSMo(O)OH] cluster in a CO dehydrogenase resolved at 1.1-Å resolution
    • Dobbek H., Gremer L., Kiefersauer R., Huber R., and Meyer O. Catalysis at a dinuclear [CuSMo(O)OH] cluster in a CO dehydrogenase resolved at 1.1-Å resolution. Proc. Natl Acad. Sci. USA 99 (2002) 15971-15976
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 15971-15976
    • Dobbek, H.1    Gremer, L.2    Kiefersauer, R.3    Huber, R.4    Meyer, O.5
  • 2
    • 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. Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism. Proc. Natl Acad. Sci. USA 102 (2005) 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
  • 4
    • 32044475396 scopus 로고    scopus 로고
    • Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes
    • Strange R.W., Antonyuk S.V., Hough M.A., Doucette P.A., Valentine J.S., and Hasnain S.S. Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes. J. Mol. Biol. 356 (2006) 1152-1162
    • (2006) J. Mol. Biol. , vol.356 , pp. 1152-1162
    • Strange, R.W.1    Antonyuk, S.V.2    Hough, M.A.3    Doucette, P.A.4    Valentine, J.S.5    Hasnain, S.S.6
  • 7
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S., Ostermeier C., Ludwig B., and Michel H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376 (1995) 660-669
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 8
    • 0038670302 scopus 로고    scopus 로고
    • The interface between the biological and inorganic worlds: iron-sulfur metalloclusters
    • Rees D.C., and Howard J.P. The interface between the biological and inorganic worlds: iron-sulfur metalloclusters. Science 300 (2003) 929-931
    • (2003) Science , vol.300 , pp. 929-931
    • Rees, D.C.1    Howard, J.P.2
  • 10
    • 33846050557 scopus 로고    scopus 로고
    • Cryoradiolytic reduction of crystalline heme proteins: analysis by UV-Vis spectroscopy and X-ray crystallography
    • Beitlich T., Kuhnel K., Schulze-Briese C., Shoeman R.L., and Schlichting I. Cryoradiolytic reduction of crystalline heme proteins: analysis by UV-Vis spectroscopy and X-ray crystallography. J. Synchrotron Radiat. 14 (2006) 11-23
    • (2006) J. Synchrotron Radiat. , vol.14 , pp. 11-23
    • Beitlich, T.1    Kuhnel, K.2    Schulze-Briese, C.3    Shoeman, R.L.4    Schlichting, I.5
  • 12
    • 0027728765 scopus 로고
    • A fast and portable microspectrophotometer for protein crystallography
    • Hadfield A.T., and Hajdu J. A fast and portable microspectrophotometer for protein crystallography. J. Appl. Crystallogr. 26 (1993) 839-842
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 839-842
    • Hadfield, A.T.1    Hajdu, J.2
  • 13
    • 33846085666 scopus 로고    scopus 로고
    • Tracking X-ray-derived redox changes in crystals of a methylamine dehydrogenase/amicyanin complex using single-crystal UV/Vis microspectrophotometry
    • Pearson A.R., Pahl R., Kovaleva E.G., Davidson V.L., and Wilmot C.M. Tracking X-ray-derived redox changes in crystals of a methylamine dehydrogenase/amicyanin complex using single-crystal UV/Vis microspectrophotometry. J. Synchrotron Radiat. 14 (2007) 92-98
    • (2007) J. Synchrotron Radiat. , vol.14 , pp. 92-98
    • Pearson, A.R.1    Pahl, R.2    Kovaleva, E.G.3    Davidson, V.L.4    Wilmot, C.M.5
  • 15
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and the molecular basis of denitrification
    • Zumft W.G. Cell biology and the molecular basis of denitrification. Microbiol. Mol. Biol. Rev. 61 (1997) 533-616
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 533-616
    • Zumft, W.G.1
  • 17
    • 0036303516 scopus 로고    scopus 로고
    • Biochemical and crystallographic studies of the Met144Ala, Asp92Asn and His254Phe mutants of the nitrite reductase from Alcaligenes xylosoxidans provide insight into the enzyme mechanism
    • Ellis M.J., Prudencio M., Dodd F.E., Strange R.W., Sawers G., Eady R.R., and Hasnain S.S. Biochemical and crystallographic studies of the Met144Ala, Asp92Asn and His254Phe mutants of the nitrite reductase from Alcaligenes xylosoxidans provide insight into the enzyme mechanism. J. Mol. Biol. 316 (2002) 51-64
    • (2002) J. Mol. Biol. , vol.316 , pp. 51-64
    • Ellis, M.J.1    Prudencio, M.2    Dodd, F.E.3    Strange, R.W.4    Sawers, G.5    Eady, R.R.6    Hasnain, S.S.7
  • 18
    • 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. Atomic resolution structures of native copper nitrite reductase from Alcaligenes xylosoxidans and the active site mutant Asp92Glu. J. Mol. Biol. 328 (2003) 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
  • 19
    • 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 Hasnain S.S. High resolution structural studies of mutants provide insights into catalysis and electron transfer processes in copper nitrite reductase. J. Mol. Biol. 350 (2005) 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    Hasnain, S.S.7
  • 20
    • 33745238976 scopus 로고    scopus 로고
    • A random-sequential mechanism for nitrite binding and active site reduction in copper-containing nitrite-reductase
    • Wijma H.J., Jeuken L.J.C., Verbeet M.P., Armstrong F.A., and Canters G.W. A random-sequential mechanism for nitrite binding and active site reduction in copper-containing nitrite-reductase. J. Biol. Chem. 281 (2006) 16340-16346
    • (2006) J. Biol. Chem. , vol.281 , pp. 16340-16346
    • Wijma, H.J.1    Jeuken, L.J.C.2    Verbeet, M.P.3    Armstrong, F.A.4    Canters, G.W.5
  • 21
    • 0242668714 scopus 로고    scopus 로고
    • Reconstitution of the type-1 active site of the H145G/A variants of nitrite reductase by ligand insertion
    • Wijma H.J., Boulanger M.J., Molon A., Fittipaldi M., Huber M., and Murphy M.E.P. Reconstitution of the type-1 active site of the H145G/A variants of nitrite reductase by ligand insertion. Biochemistry 42 (2003) 4075-4083
    • (2003) Biochemistry , vol.42 , pp. 4075-4083
    • Wijma, H.J.1    Boulanger, M.J.2    Molon, A.3    Fittipaldi, M.4    Huber, M.5    Murphy, M.E.P.6
  • 22
    • 0000720440 scopus 로고
    • Low temperature X-ray absorption spectroscopy of plastocyanin: evidence for copper site photoreduction at cryogenic temperatures
    • Penner-Hahn J.E., Murata M., Hodgson K.O., and Freeman H.C. Low temperature X-ray absorption spectroscopy of plastocyanin: evidence for copper site photoreduction at cryogenic temperatures. Inorg. Chem. 28 (1989) 1826-1832
    • (1989) Inorg. Chem. , vol.28 , pp. 1826-1832
    • Penner-Hahn, J.E.1    Murata, M.2    Hodgson, K.O.3    Freeman, H.C.4
  • 23
    • 0001921412 scopus 로고
    • Quick Fluorescence EXAFS: an improved method for data collection of conventional XAFS data and for studying reaction intermediates in dilute systems
    • Murphy L.M., Dobson B.R., Neu M., Ramsdale C.A., Strange R.W., and Hasnain S.S. Quick Fluorescence EXAFS: an improved method for data collection of conventional XAFS data and for studying reaction intermediates in dilute systems. J. Synchrotron Radiat. 2 (1995) 64-69
    • (1995) J. Synchrotron Radiat. , vol.2 , pp. 64-69
    • Murphy, L.M.1    Dobson, B.R.2    Neu, M.3    Ramsdale, C.A.4    Strange, R.W.5    Hasnain, S.S.6
  • 25
    • 0032475972 scopus 로고    scopus 로고
    • The intramolecular electron transfer between copper sites of nitrite reductase: a comparison with ascorbate oxidase
    • Farver O., Eady R.R., Abraham Z.H.L., and Pecht I. The intramolecular electron transfer between copper sites of nitrite reductase: a comparison with ascorbate oxidase. FEBS Lett. 436 (1998) 239-242
    • (1998) FEBS Lett. , vol.436 , pp. 239-242
    • Farver, O.1    Eady, R.R.2    Abraham, Z.H.L.3    Pecht, I.4
  • 26
    • 0001175679 scopus 로고    scopus 로고
    • Intramolecular electron-transfer process of native and mutant forms of blue copper-containing nitrite reductase from Alcaligenes xylosoxidans
    • Suzuki S., Furusawa H., Kataoka K., Yamaguchi K., Kobayashi K., and Tagawa S. Intramolecular electron-transfer process of native and mutant forms of blue copper-containing nitrite reductase from Alcaligenes xylosoxidans. Inorg. React. Mech. 2 (2000) 129-135
    • (2000) Inorg. React. Mech. , vol.2 , pp. 129-135
    • Suzuki, S.1    Furusawa, H.2    Kataoka, K.3    Yamaguchi, K.4    Kobayashi, K.5    Tagawa, S.6
  • 27
    • 0037072806 scopus 로고    scopus 로고
    • {radical dot}- radical binds to the substrate binding type 2 copper site before the type 2 copper is reduced
    • {radical dot}- radical binds to the substrate binding type 2 copper site before the type 2 copper is reduced. J. Biol. Chem. 277 (2002) 34067-34073
    • (2002) J. Biol. Chem. , vol.277 , pp. 34067-34073
    • Yousafzai, F.K.1    Eady, R.R.2
  • 28
    • 0040631692 scopus 로고    scopus 로고
    • Structure of metal centres in proteins at subatomic resolution
    • Hasnain S.S., and Hodgson K.O. Structure of metal centres in proteins at subatomic resolution. J. Synchrotron Radiat. 6 (1999) 852-864
    • (1999) J. Synchrotron Radiat. , vol.6 , pp. 852-864
    • Hasnain, S.S.1    Hodgson, K.O.2
  • 29
    • 0034129580 scopus 로고    scopus 로고
    • 3D EXAFS refinement of the Cu site of azurin sheds light on the nature of structural change at the metal centre in an oxidation-reduction process: an integrated approach combining EXAFS and crystallography
    • Cheung K.C., Strange R.W., and Hasnain S.S. 3D EXAFS refinement of the Cu site of azurin sheds light on the nature of structural change at the metal centre in an oxidation-reduction process: an integrated approach combining EXAFS and crystallography. Acta Crystallogr. Sect. D 56 (2000) 697-704
    • (2000) Acta Crystallogr. Sect. D , vol.56 , pp. 697-704
    • Cheung, K.C.1    Strange, R.W.2    Hasnain, S.S.3
  • 30
    • 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.P. Side-on copper-nitrosyl coordination by nitrite reductase. Science 304 (2004) 867-870
    • (2004) Science , vol.304 , pp. 867-870
    • Tocheva, E.I.1    Rosell, F.I.2    Mauk, A.G.3    Murphy, M.E.P.4
  • 31
    • 34250378756 scopus 로고    scopus 로고
    • pH dependence of copper geometry, reduction potential, and nitrite affinity in nitrite reductase
    • Jacobson F., Pistorius A., Farkas D., De Grip W., Hansson O., Sjolin L., and Neutze R. pH dependence of copper geometry, reduction potential, and nitrite affinity in nitrite reductase. J. Biol. Chem. 282 (2007) 6347-6355
    • (2007) J. Biol. Chem. , vol.282 , pp. 6347-6355
    • Jacobson, F.1    Pistorius, A.2    Farkas, D.3    De Grip, W.4    Hansson, O.5    Sjolin, L.6    Neutze, R.7
  • 32
    • 0344573109 scopus 로고    scopus 로고
    • The blue copper-containing nitrite reductase from Alcaligenes xylosoxidans: cloning of the nirA gene and characterization of the recombinant enzyme
    • Prudencio M., Eady R.R., and Sawers G. The blue copper-containing nitrite reductase from Alcaligenes xylosoxidans: cloning of the nirA gene and characterization of the recombinant enzyme. J. Bacteriol. 181 (1999) 2323-2329
    • (1999) J. Bacteriol. , vol.181 , pp. 2323-2329
    • Prudencio, M.1    Eady, R.R.2    Sawers, G.3
  • 33
    • 23844522625 scopus 로고    scopus 로고
    • A high-throughput structural biology/proteomics beamline at the SRS on a new multipole wiggler
    • Cianci M., Antonyuk S., Bliss N., Bailey M.W., Buffey S.G., Cheung K.C., et al. A high-throughput structural biology/proteomics beamline at the SRS on a new multipole wiggler. J. Synchrotron Radiat. 12 (2005) 455-466
    • (2005) J. Synchrotron Radiat. , vol.12 , pp. 455-466
    • Cianci, M.1    Antonyuk, S.2    Bliss, N.3    Bailey, M.W.4    Buffey, S.G.5    Cheung, K.C.6
  • 34
    • 0033464412 scopus 로고    scopus 로고
    • A low-profile monolithic multi-element Ge detector for X-ray fluorescence applications
    • Derbyshire G., Kan-Cheung C., Sansingkeow P., and Hasnain S.S. A low-profile monolithic multi-element Ge detector for X-ray fluorescence applications. J. Synchrotron Radiat. 6 (1999) 62-63
    • (1999) J. Synchrotron Radiat. , vol.6 , pp. 62-63
    • Derbyshire, G.1    Kan-Cheung, C.2    Sansingkeow, P.3    Hasnain, S.S.4
  • 35
    • 4043099008 scopus 로고    scopus 로고
    • X-ray absorption by macromolecular crystals: the effects of wavelength and crystal composition on absorbed dose
    • Murray J.W., Garman E.F., and Ravelli R.B.G. X-ray absorption by macromolecular crystals: the effects of wavelength and crystal composition on absorbed dose. J. Appl. Crystallogr. 37 (2004) 513-522
    • (2004) J. Appl. Crystallogr. , vol.37 , pp. 513-522
    • Murray, J.W.1    Garman, E.F.2    Ravelli, R.B.G.3
  • 36
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D 53 (1997) 240-255
    • (1997) Acta Crystallogr. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 37
    • 13244281317 scopus 로고    scopus 로고
    • COOT: model-building tools for molecular graphics
    • Emsley P., and Cowtan K.D. COOT: model-building tools for molecular graphics. Acta Crystallogr. Sect. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. Sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.D.2
  • 38
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris R.J., Perrakis A., and Lamzin V.S. ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol. 374 (2003) 229-244
    • (2003) Methods Enzymol. , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 39


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