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Volumn 113, Issue 11, 2016, Pages 2928-2933

Redox-coupled proton transfer mechanism in nitrite reductase revealed by femtosecond crystallography

(22)  Fukuda, Yohta a,b   Tse, Ka Man a   Nakane, Takanori c   Nakatsu, Toru d,e   Suzuki, Mamoru a,e   Sugahara, Michihiro e   Inoue, Shigeyuki e,f   Masuda, Tetsuya d,e   Yumoto, Fumiaki g   Matsugaki, Naohiro g   Nango, Eriko e   Tono, Kensuke h   Joti, Yasumasa h   Kameshima, Takashi h   Song, Changyong e,i   Hatsui, Takaki e   Yabashi, Makina e   Nureki, Osamu e,j   Murphy, Michael E P d   Inoue, Tsuyoshi a   more..

i RIKEN   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN; HYDROXYL GROUP; NITRITE REDUCTASE; BACTERIAL PROTEIN; COPPER; HYBRID PROTEIN; NITRITE; NITRITE REDUCTASE, COPPER-CONTAINING; PROTON;

EID: 84962320904     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1517770113     Document Type: Article
Times cited : (87)

References (72)
  • 1
    • 44249109495 scopus 로고    scopus 로고
    • Transformation of the nitrogen cycle: Recent trends, questions, and potential solutions
    • Galloway JN, et al. (2008) Transformation of the nitrogen cycle: Recent trends, questions, and potential solutions. Science 320(5878):889-892.
    • (2008) Science , vol.320 , Issue.5878 , pp. 889-892
    • Galloway, J.N.1
  • 2
    • 38349190507 scopus 로고    scopus 로고
    • An Earth-system perspective of the global nitrogen cycle
    • Gruber N, Galloway JN (2008) An Earth-system perspective of the global nitrogen cycle. Nature 451(7176):293-296.
    • (2008) Nature , vol.451 , Issue.7176 , pp. 293-296
    • Gruber, N.1    Galloway, J.N.2
  • 3
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and molecular basis of denitrification
    • Zumft WG (1997) Cell biology and molecular basis of denitrification. Microbiol Mol Biol Rev 61(4):533-616.
    • (1997) Microbiol Mol Biol Rev , vol.61 , Issue.4 , pp. 533-616
    • Zumft, W.G.1
  • 5
    • 0029054793 scopus 로고
    • The anatomy of a bifunctional enzyme: Structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1
    • Fülöp V, Moir JWB, Ferguson SJ, Hajdu J (1995) The anatomy of a bifunctional enzyme: Structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1. Cell 81(3):369-377.
    • (1995) Cell , vol.81 , Issue.3 , pp. 369-377
    • Fülöp, V.1    Moir, J.W.B.2    Ferguson, S.J.3    Hajdu, J.4
  • 6
    • 1842412487 scopus 로고    scopus 로고
    • Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme
    • Williams PA, et al. (1997) Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme. Nature 389(6649):406-412.
    • (1997) Nature , vol.389 , Issue.6649 , pp. 406-412
    • Williams, P.A.1
  • 7
    • 84858016892 scopus 로고    scopus 로고
    • Binding and activation of nitrite and nitric oxide by copper nitrite reductase and corresponding model complexes
    • Merkle AC, Lehnert N (2012) Binding and activation of nitrite and nitric oxide by copper nitrite reductase and corresponding model complexes. Dalton Trans 41(12):3355-3368.
    • (2012) Dalton Trans , vol.41 , Issue.12 , pp. 3355-3368
    • Merkle, A.C.1    Lehnert, N.2
  • 8
    • 0026353602 scopus 로고
    • The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes
    • Godden JW, et al. (1991) The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes. Science 253(5018):438-442.
    • (1991) Science , vol.253 , Issue.5018 , pp. 438-442
    • Godden, J.W.1
  • 9
    • 0033574613 scopus 로고    scopus 로고
    • Structural and kinetic evidence for an ordered mechanism of copper nitrite reductase
    • Strange RW, et al. (1999) Structural and kinetic evidence for an ordered mechanism of copper nitrite reductase. J Mol Biol 287(5):1001-1009.
    • (1999) J Mol Biol , vol.287 , Issue.5 , pp. 1001-1009
    • Strange, R.W.1
  • 10
    • 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, 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(2):345-350.
    • (2000) J Biochem , vol.127 , Issue.2 , pp. 345-350
    • Kataoka, K.1    Furusawa, H.2    Takagi, K.3    Yamaguchi, K.4    Suzuki, S.5
  • 11
    • 0034604550 scopus 로고    scopus 로고
    • Catalytic roles for two water bridged residues (Asp-98 and His-255) in the active site of coppercontaining nitrite reductase
    • Boulanger MJ, Kukimoto M, Nishiyama M, Horinouchi S, Murphy ME (2000) Catalytic roles for two water bridged residues (Asp-98 and His-255) in the active site of coppercontaining nitrite reductase. J Biol Chem 275(31):23957-23964.
    • (2000) J Biol Chem , vol.275 , Issue.31 , pp. 23957-23964
    • Boulanger, M.J.1    Kukimoto, M.2    Nishiyama, M.3    Horinouchi, S.4    Murphy, M.E.5
  • 12
    • 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 MJ, Murphy MEP (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(31):9132-9141.
    • (2001) Biochemistry , vol.40 , Issue.31 , pp. 9132-9141
    • Boulanger, M.J.1    Murphy, M.E.P.2
  • 13
    • 33745238976 scopus 로고    scopus 로고
    • A randomsequential mechanism for nitrite binding and active site reduction in copper-containing nitrite reductase
    • Wijma HJ, Jeuken LJ, Verbeet MP, Armstrong FA, Canters GW (2006) A randomsequential mechanism for nitrite binding and active site reduction in copper-containing nitrite reductase. J Biol Chem 281(24):16340-16346.
    • (2006) J Biol Chem , vol.281 , Issue.24 , pp. 16340-16346
    • Wijma, H.J.1    Jeuken, L.J.2    Verbeet, M.P.3    Armstrong, F.A.4    Canters, G.W.5
  • 14
    • 34447530736 scopus 로고    scopus 로고
    • Protein film voltammetry of copper-containing nitrite reductase reveals reversible inactivation
    • Wijma HJ, Jeuken LJC, Verbeet MP, Armstrong FA, Canters GW (2007) Protein film voltammetry of copper-containing nitrite reductase reveals reversible inactivation. J Am Chem Soc 129(27):8557-8565.
    • (2007) J Am Chem Soc , vol.129 , Issue.27 , pp. 8557-8565
    • Wijma, H.J.1    Jeuken, L.J.C.2    Verbeet, M.P.3    Armstrong, F.A.4    Canters, G.W.5
  • 15
    • 0032839514 scopus 로고    scopus 로고
    • The pH-dependent changes of intramolecular electron transfer on copper-containing nitrite reductase
    • Kobayashi K, Tagawa S, Deligeer, Suzuki S (1999) The pH-dependent changes of intramolecular electron transfer on copper-containing nitrite reductase. J Biochem 126(2):408-412.
    • (1999) J Biochem , vol.126 , Issue.2 , pp. 408-412
    • Kobayashi, K.1    Tagawa, S.2    Deligeer3    Suzuki, S.4
  • 16
    • 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, et al. (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(17):6086-6094.
    • (1998) Biochemistry , vol.37 , Issue.17 , pp. 6086-6094
    • Olesen, K.1
  • 17
    • 79955811857 scopus 로고    scopus 로고
    • Proton-coupled electron transfer in the catalytic cycle of Alcaligenes xylosoxidans copper-dependent nitrite reductase
    • Leferink NG, et al. (2011) Proton-coupled electron transfer in the catalytic cycle of Alcaligenes xylosoxidans copper-dependent nitrite reductase. Biochemistry 50(19):4121-4131.
    • (2011) Biochemistry , vol.50 , Issue.19 , pp. 4121-4131
    • Leferink, N.G.1
  • 18
    • 70350025521 scopus 로고    scopus 로고
    • Demonstration of proton-coupled electron transfer in the copper-containing nitrite reductases
    • Brenner S, et al. (2009) Demonstration of proton-coupled electron transfer in the copper-containing nitrite reductases. J Biol Chem 284(38):25973-25983.
    • (2009) J Biol Chem , vol.284 , Issue.38 , pp. 25973-25983
    • Brenner, S.1
  • 19
    • 27844519543 scopus 로고    scopus 로고
    • Structures of the oxidized and reduced forms of nitrite reductase from Rhodobacter sphaeroides 2.4.3 at high pH: Changes in the interactions of the type 2 copper
    • Jacobson F, et al. (2005) Structures of the oxidized and reduced forms of nitrite reductase from Rhodobacter sphaeroides 2.4.3 at high pH: Changes in the interactions of the type 2 copper. Acta Crystallogr D Biol Crystallogr 61(Pt 9):1190-1198.
    • (2005) Acta Crystallogr D Biol Crystallogr , vol.61 , pp. 1190-1198
    • Jacobson, F.1
  • 20
    • 34250378756 scopus 로고    scopus 로고
    • PH dependence of copper geometry, reduction potential, and nitrite affinity in nitrite reductase
    • Jacobson F, et al. (2007) pH dependence of copper geometry, reduction potential, and nitrite affinity in nitrite reductase. J Biol Chem 282(9):6347-6355.
    • (2007) J Biol Chem , vol.282 , Issue.9 , pp. 6347-6355
    • Jacobson, F.1
  • 21
    • 41249101880 scopus 로고    scopus 로고
    • Crystallography with online optical and X-ray absorption spectroscopies demonstrates an ordered mechanism in copper nitrite reductase
    • Hough MA, Antonyuk SV, Strange RW, Eady RR, Hasnain SS (2008) Crystallography with online optical and X-ray absorption spectroscopies demonstrates an ordered mechanism in copper nitrite reductase. J Mol Biol 378(2):353-361.
    • (2008) J Mol Biol , vol.378 , Issue.2 , pp. 353-361
    • Hough, M.A.1    Antonyuk, S.V.2    Strange, R.W.3    Eady, R.R.4    Hasnain, S.S.5
  • 22
    • 2442604589 scopus 로고    scopus 로고
    • Side-on copper-nitrosyl coordination by nitrite reductase
    • Tocheva EI, Rosell FI, Mauk AG, Murphy ME (2004) Side-on copper-nitrosyl coordination by nitrite reductase. Science 304(5672):867-870.
    • (2004) Science , vol.304 , Issue.5672 , pp. 867-870
    • Tocheva, E.I.1    Rosell, F.I.2    Mauk, A.G.3    Murphy, M.E.4
  • 23
    • 24744467360 scopus 로고    scopus 로고
    • Atomic resolution structures of resting-state, substrate- And product-complexed Cu-nitrite reductase provide insight into catalytic mechanism
    • Antonyuk SV, Strange RW, Sawers G, Eady RR, Hasnain SS (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(34):12041-12046.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.34 , pp. 12041-12046
    • Antonyuk, S.V.1    Strange, R.W.2    Sawers, G.3    Eady, R.R.4    Hasnain, S.S.5
  • 24
    • 42049123859 scopus 로고    scopus 로고
    • Conserved active site residues limit inhibition of a copper-containing nitrite reductase by small molecules
    • Tocheva EI, Eltis LD, Murphy MEP (2008) Conserved active site residues limit inhibition of a copper-containing nitrite reductase by small molecules. Biochemistry 47(15):4452-4460.
    • (2008) Biochemistry , vol.47 , Issue.15 , pp. 4452-4460
    • Tocheva, E.I.1    Eltis, L.D.2    Murphy, M.E.P.3
  • 25
    • 35649012654 scopus 로고    scopus 로고
    • Stable copper-nitrosyl formation by nitrite reductase in either oxidation state
    • Tocheva EI, Rosell FI, Mauk AG, Murphy MEP (2007) Stable copper-nitrosyl formation by nitrite reductase in either oxidation state. Biochemistry 46(43):12366-12374.
    • (2007) Biochemistry , vol.46 , Issue.43 , pp. 12366-12374
    • Tocheva, E.I.1    Rosell, F.I.2    Mauk, A.G.3    Murphy, M.E.P.4
  • 26
    • 0027950819 scopus 로고
    • Reductive disproportionation of NO mediated by copper complexes: Modeling N, O generation by copper proteins and heterogeneous catalyst
    • Ruggiero CE, Carrier SM, Tolman WB (1994) Reductive disproportionation of NO mediated by copper complexes: Modeling N, O generation by copper proteins and heterogeneous catalyst. Angew Chem Int Ed Engl 33(8):895-897.
    • (1994) Angew Chem Int Ed Engl , vol.33 , Issue.8 , pp. 895-897
    • Ruggiero, C.E.1    Carrier, S.M.2    Tolman, W.B.3
  • 27
    • 2742588224 scopus 로고    scopus 로고
    • Synthesis, structure, and reactivity of model complexes of copper nitrite reductase
    • Casella L, Carugo O, Gullotti M, Doldi S, Frassoni M(1996) Synthesis, structure, and reactivity of model complexes of copper nitrite reductase. Inorg Chem 35(5):1101-1113.
    • (1996) Inorg Chem , vol.35 , Issue.5 , pp. 1101-1113
    • Casella, L.1    Carugo, O.2    Gullotti, M.3    Doldi, S.4    Frassoni, M.5
  • 28
    • 17844387111 scopus 로고    scopus 로고
    • CuI and CuII complexes containing nitrite and tridentate aromatic amine ligand as models for the substratebinding type-2 Cu site of nitrite reductase
    • Yokoyama H, Yamaguchi K, Sugimoto M, Suzuki S (2005) CuI and CuII complexes containing nitrite and tridentate aromatic amine ligand as models for the substratebinding type-2 Cu site of nitrite reductase. Eur J Inorg Chem 8:1435-1441.
    • (2005) Eur J Inorg Chem , vol.8 , pp. 1435-1441
    • Yokoyama, H.1    Yamaguchi, K.2    Sugimoto, M.3    Suzuki, S.4
  • 29
    • 34249705142 scopus 로고    scopus 로고
    • Synthesis and spectroscopic characterization of copper(II)- nitrito complexes with hydrotris(pyrazolyl)borate and related coligands
    • Lehnert N, et al. (2007) Synthesis and spectroscopic characterization of copper(II)- nitrito complexes with hydrotris(pyrazolyl)borate and related coligands. Inorg Chem 46(10):3916-3933.
    • (2007) Inorg Chem , vol.46 , Issue.10 , pp. 3916-3933
    • Lehnert, N.1
  • 30
    • 0034088779 scopus 로고    scopus 로고
    • The catalytic pathway of cytochrome p450cam at atomic resolution
    • Schlichting I, et al. (2000) The catalytic pathway of cytochrome p450cam at atomic resolution. Science 287(5458):1615-1622.
    • (2000) Science , vol.287 , Issue.5458 , pp. 1615-1622
    • Schlichting, I.1
  • 31
    • 0037161809 scopus 로고    scopus 로고
    • The catalytic pathway of horseradish peroxidase at high resolution
    • Berglund GI, et al. (2002) The catalytic pathway of horseradish peroxidase at high resolution. Nature 417(6887):463-468.
    • (2002) Nature , vol.417 , Issue.6887 , pp. 463-468
    • Berglund, G.I.1
  • 32
    • 79955812240 scopus 로고    scopus 로고
    • Monitoring and validating active site redox states in protein crystals
    • Antonyuk SV, Hough MA (2011) Monitoring and validating active site redox states in protein crystals. Biochim Biophys Acta 1814(6):778-784.
    • (2011) Biochim Biophys Acta , vol.1814 , Issue.6 , pp. 778-784
    • Antonyuk, S.V.1    Hough, M.A.2
  • 33
    • 71449103005 scopus 로고    scopus 로고
    • Hidden alternative structures of proline isomerase essential for catalysis
    • Fraser JS, et al. (2009) Hidden alternative structures of proline isomerase essential for catalysis. Nature 462(7273):669-673.
    • (2009) Nature , vol.2462 , Issue.7273 , pp. 669-673
    • Fraser, J.S.1
  • 34
    • 80053626537 scopus 로고    scopus 로고
    • Accessing protein conformational ensembles using roomtemperature X-ray crystallography
    • Fraser JS, et al. (2011) Accessing protein conformational ensembles using roomtemperature X-ray crystallography. Proc Natl Acad Sci USA 108(39):16247-16252.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.39 , pp. 16247-16252
    • Fraser, J.S.1
  • 35
    • 84902319994 scopus 로고    scopus 로고
    • Crystal cryocooling distorts conformational heterogeneity in a model Michaelis complex of DHF
    • R
    • Keedy DA, et al. (2014) Crystal cryocooling distorts conformational heterogeneity in a model Michaelis complex of DHFR. Structure 22(6):899-910.
    • (2014) Structure , vol.22 , Issue.6 , pp. 899-910
    • Keedy, D.A.1
  • 36
    • 84926435303 scopus 로고    scopus 로고
    • High-temperature and high-resolution crystallography of thermostable copper nitrite reductase
    • Fukuda Y, Inoue T (2015) High-temperature and high-resolution crystallography of thermostable copper nitrite reductase. Chem Commun (Camb) 51(30):6532-6535.
    • (2015) Chem Commun (Camb) , vol.51 , Issue.30 , pp. 6532-6535
    • Fukuda, Y.1    Inoue, T.2
  • 37
    • 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 AC, 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(24):11504-11506.
    • (2009) Inorg Chem , vol.48 , Issue.24 , pp. 11504-11506
    • Merkle, A.C.1    Lehnert, N.2
  • 39
    • 34548236944 scopus 로고    scopus 로고
    • Resolution of the spectroscopy versus crystallography issue for NO intermediates of nitrite reductase from Rhodobacter sphaeroides
    • Ghosh S, et al. (2007) Resolution of the spectroscopy versus crystallography issue for NO intermediates of nitrite reductase from Rhodobacter sphaeroides. J Am Chem Soc 129(34):10310-10311.
    • (2007) J Am Chem Soc , vol.129 , Issue.34 , pp. 10310-10311
    • Ghosh, S.1
  • 40
    • 38649141501 scopus 로고    scopus 로고
    • Structural and spectroscopic characterization of mononuclear copper(I) nitrosyl complexes: End-on versus side-on coordination of NO to copper(I)
    • Fujisawa K, et al. (2008) Structural and spectroscopic characterization of mononuclear copper(I) nitrosyl complexes: End-on versus side-on coordination of NO to copper(I). J Am Chem Soc 130(4):1205-1213.
    • (2008) J Am Chem Soc , vol.130 , Issue.4 , pp. 1205-1213
    • Fujisawa, K.1
  • 41
    • 79551658540 scopus 로고    scopus 로고
    • Femtosecond X-ray protein nanocrystallography
    • Chapman HN, et al. (2011) Femtosecond X-ray protein nanocrystallography. Nature 470(7332):73-77.
    • (2011) Nature , vol.470 , Issue.7332 , pp. 73-77
    • Chapman, H.N.1
  • 42
    • 84862545637 scopus 로고    scopus 로고
    • Room temperature femtosecond X-ray diffraction of photosystem II microcrystals
    • Kern J, et al. (2012) Room temperature femtosecond X-ray diffraction of photosystem II microcrystals. Proc Natl Acad Sci USA 109(25):9721-9726.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.25 , pp. 9721-9726
    • Kern, J.1
  • 43
    • 84890950819 scopus 로고    scopus 로고
    • Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography
    • Johansson LC, et al. (2013) Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography. Nat Commun 4:2911.
    • (2013) Nat Commun , vol.4 , pp. 2911
    • Johansson, L.C.1
  • 44
    • 84890840505 scopus 로고    scopus 로고
    • Serial femtosecond crystallography of G protein-coupled receptors
    • Liu W, et al. (2013) Serial femtosecond crystallography of G protein-coupled receptors. Science 342(6165):1521-1524.
    • (2013) Science , vol.342 , Issue.6165 , pp. 1521-1524
    • Liu, W.1
  • 45
    • 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, Beppu T (1981) Purification and properties of a copper-containing nitrite reductase from a denitrifying bacterium, Alcaligenes faecalis strain S-6. J Biochem 89(2):453-461.
    • (1981) J Biochem , vol.89 , Issue.2 , pp. 453-461
    • Kakutani, T.1    Watanabe, H.2    Arima, K.3    Beppu, T.4
  • 46
    • 0030658026 scopus 로고    scopus 로고
    • Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications
    • Murphy MEP, Turley S, Adman ET (1997) Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications. J Biol Chem 272(45):28455-28460.
    • (1997) J Biol Chem , vol.272 , Issue.45 , pp. 28455-28460
    • Murphy, M.E.P.1    Turley, S.2    Adman, E.T.3
  • 47
    • 1542378734 scopus 로고    scopus 로고
    • Electronic structures of metal sites in proteins and models: Contributions to function in blue copper proteins
    • Solomon EI, Szilagyi RK, DeBeer George S, Basumallick L (2004) Electronic structures of metal sites in proteins and models: Contributions to function in blue copper proteins. Chem Rev 104(2):419-458.
    • (2004) Chem Rev , vol.104 , Issue.2 , pp. 419-458
    • Solomon, E.I.1    Szilagyi, R.K.2    DeBeer, G.S.3    Basumallick, L.4
  • 48
    • 84948807304 scopus 로고    scopus 로고
    • Native sulfur/chlorine SAD phasing for serial femtosecond crystallography
    • Nakane T, et al. (2015) Native sulfur/chlorine SAD phasing for serial femtosecond crystallography. Acta Crystallogr D Biol Crystallogr 71(Pt 12):2519-2525.
    • (2015) Acta Crystallogr D Biol Crystallogr , vol.71 , pp. 2519-2525
    • Nakane, T.1
  • 49
    • 62649090829 scopus 로고    scopus 로고
    • Spectroscopic and computational studies of nitrite reductase: Proton induced electron transfer and backbonding contributions to reactivity
    • Ghosh S, Dey A, Sun Y, Scholes CP, Solomon EI (2009) Spectroscopic and computational studies of nitrite reductase: Proton induced electron transfer and backbonding contributions to reactivity. J Am Chem Soc 131(1):277-288.
    • (2009) J Am Chem Soc , vol.131 , Issue.1 , pp. 277-288
    • Ghosh, S.1    Dey, A.2    Sun, Y.3    Scholes, C.P.4    Solomon, E.I.5
  • 50
    • 0028140633 scopus 로고
    • Synthetic model of the substrate adduct to the reduced active site of copper nitrite reductase
    • Halfen JA, Tolman WB (1994) Synthetic model of the substrate adduct to the reduced active site of copper nitrite reductase. J Am Chem Soc 116:5475-5476.
    • (1994) J Am Chem Soc , vol.116 , pp. 5475-5476
    • Halfen, J.A.1    Tolman, W.B.2
  • 51
    • 0030066250 scopus 로고    scopus 로고
    • Synthetic modeling of nitrite binding and activation by reduced copper proteins. Characterization of copper(I)-nitrite complexes that evolve nitric oxide
    • Halfen JA, et al. (1996) Synthetic modeling of nitrite binding and activation by reduced copper proteins. Characterization of copper(I)-nitrite complexes that evolve nitric oxide. J Am Chem Soc 118:763-776.
    • (1996) J Am Chem Soc , vol.118 , pp. 763-776
    • Halfen, J.A.1
  • 52
    • 43249103478 scopus 로고    scopus 로고
    • Effect of a tridentate ligand on the structure, electronic structure, and reactivity of the copper(I) nitrite complex: Role of the conserved three-histidine ligand environment of the type-2 copper site in copper-containing nitrite reductases
    • Kujime M, Izumi C, Tomura M, Hada M, Fujii H (2008) Effect of a tridentate ligand on the structure, electronic structure, and reactivity of the copper(I) nitrite complex: Role of the conserved three-histidine ligand environment of the type-2 copper site in copper-containing nitrite reductases. J Am Chem Soc 130(19):6088-6098.
    • (2008) J Am Chem Soc , vol.130 , Issue.19 , pp. 6088-6098
    • Kujime, M.1    Izumi, C.2    Tomura, M.3    Hada, M.4    Fujii, H.5
  • 53
    • 84922672281 scopus 로고    scopus 로고
    • Enzymatic mechanism of copper-containing nitrite reductase
    • Li Y, Hodak M, Bernholc J (2015) Enzymatic mechanism of copper-containing nitrite reductase. Biochemistry 54(5):1233-1242.
    • (2015) Biochemistry , vol.54 , Issue.5 , pp. 1233-1242
    • Li, Y.1    Hodak, M.2    Bernholc, J.3
  • 54
    • 0016853331 scopus 로고
    • Protein crystallography at sub-zero temperatures: Lysozyme-substrate complexes in cooled mixed solvents
    • Douzou P, Hoa GHB, Petsko GA (1975) Protein crystallography at sub-zero temperatures: Lysozyme-substrate complexes in cooled mixed solvents. J Mol Biol 96(3):367-380.
    • (1975) J Mol Biol , vol.96 , Issue.3 , pp. 367-380
    • Douzou, P.1    Hoa, G.H.B.2    Petsko, G.A.3
  • 55
    • 84966397505 scopus 로고    scopus 로고
    • Redox-coupled structural changes in nitrite reductase revealed by serial femtosecond and microfocus crystallography
    • Fukuda Y, et al. (2016) Redox-coupled structural changes in nitrite reductase revealed by serial femtosecond and microfocus crystallography. J Biochemmvv 133.
    • (2016) J Biochemmvv , pp. 133
    • Fukuda, Y.1
  • 56
    • 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 MJ, Murphy MEP (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(5):1111-1127.
    • (2002) J Mol Biol , vol.315 , Issue.5 , pp. 1111-1127
    • Boulanger, M.J.1    Murphy, M.E.P.2
  • 57
    • 84883444522 scopus 로고    scopus 로고
    • Characterization of a nitrite reductase involved in nitrifier denitrification
    • Lawton TJ, Bowen KE, Sayavedra-Soto LA, Arp DJ, Rosenzweig AC (2013) Characterization of a nitrite reductase involved in nitrifier denitrification. J Biol Chem 288(35):25575-25583.
    • (2013) J Biol Chem , vol.288 , Issue.35 , pp. 25575-25583
    • Lawton, T.J.1    Bowen, K.E.2    Sayavedra-Soto, L.A.3    Arp, D.J.4    Rosenzweig, A.C.5
  • 58
    • 0034319668 scopus 로고    scopus 로고
    • Carbon monoxide binding to copper-containing nitrite reductase from Alcaligenes faecalis
    • Zhang H, Boulanger MJ, Mauk AG, Murphy MEP (2000) Carbon 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.1    Boulanger, M.J.2    Mauk, A.G.3    Murphy, M.E.P.4
  • 59
    • 84893249131 scopus 로고    scopus 로고
    • Structural insights into the function of a thermostable coppercontaining nitrite reductase
    • Fukuda Y, et al. (2014) Structural insights into the function of a thermostable coppercontaining nitrite reductase. J Biochem 155(2):123-135.
    • (2014) J Biochem , vol.155 , Issue.2 , pp. 123-135
    • Fukuda, Y.1
  • 60
    • 84918582756 scopus 로고    scopus 로고
    • Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein
    • Tenboer J, et al. (2014) Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein. Science 346(6214):1242-1246.
    • (2014) Science , vol.346 , Issue.6214 , pp. 1242-1246
    • Tenboer, J.1
  • 61
    • 84906087743 scopus 로고    scopus 로고
    • Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser
    • Kupitz C, et al. (2014) Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser. Nature 513(7517):261-265.
    • (2014) Nature , vol.513 , Issue.7517 , pp. 261-265
    • Kupitz, C.1
  • 62
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, 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
  • 63
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy AJ, et al. (2007) Phaser crystallographic software. J Appl Cryst 40(Pt 4):658-674.
    • (2007) J Appl Cryst , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 65
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov GN, et al. (2011) REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr D Biol Crystallogr 67(Pt 4):355-367.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 355-367
    • Murshudov, G.N.1
  • 66
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn MD, et al. (2011) Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr 67(Pt 4):235-242.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 67
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen VB, et al. (2010) MolProbity: All-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66(Pt 1):12-21.
    • (2010) Acta Crystallogr D Biol, Crystallogr , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 68
    • 84922623231 scopus 로고    scopus 로고
    • Grease matrix as a versatile carrier of proteins for serial crystallography
    • Sugahara M, et al. (2015) Grease matrix as a versatile carrier of proteins for serial crystallography. Nat Methods 12(1):61-63.
    • (2015) Nat Methods , vol.12 , Issue.1 , pp. 61-63
    • Sugahara, M.1
  • 69
    • 84883409581 scopus 로고    scopus 로고
    • Beamline, experimental stations and photon beam diagnostics for the hard x-ray free electron laser of SACLA
    • Tono K, et al. (2013) Beamline, experimental stations and photon beam diagnostics for the hard x-ray free electron laser of SACLA. New J Phys 15(8):083035.
    • (2013) New J Phys , vol.15 , Issue.8 , pp. 083035
    • Tono, K.1
  • 70
    • 84859777150 scopus 로고    scopus 로고
    • CrystFEL: A software suite for snapshot serial crystallography
    • White TA, et al. (2012) CrystFEL: A software suite for snapshot serial crystallography. J Appl Cryst 45(2):335-341.
    • (2012) J Appl Cryst , vol.45 , Issue.2 , pp. 335-341
    • White, T.A.1
  • 71
    • 0026853348 scopus 로고
    • Indexing in single-crystal diffractometry with an obstinate list of reflections
    • Duisenberg AJM (1992) Indexing in single-crystal diffractometry with an obstinate list of reflections. J Appl Cryst 25:92-96.
    • (1992) J Appl Cryst , vol.25 , pp. 92-96
    • Duisenberg, A.J.M.1
  • 72
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification
    • Sheldrick GM (2010) Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification. Acta Crystallogr D Biol Crystallogr 66(Pt 4):479-485.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 479-485
    • Sheldrick, G.M.1


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