메뉴 건너뛰기




Volumn 109, Issue 52, 2012, Pages 21234-21239

Designing a functional type 2 copper center that has nitrite reductase activity within α-helical coiled coils

Author keywords

NiR; NO; TRI peptides

Indexed keywords

ASCORBIC ACID; COPPER; HISTIDINE; NITRIC OXIDE; NITRITE; NITRITE REDUCTASE; WATER;

EID: 84871833446     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1212893110     Document Type: Article
Times cited : (94)

References (60)
  • 1
    • 68949195832 scopus 로고    scopus 로고
    • Design of functional metalloproteins
    • Lu Y, Yeung N, Sieracki N, Marshall NM (2009) Design of functional metalloproteins. Nature 460(7257):855-862.
    • (2009) Nature , vol.460 , Issue.7257 , pp. 855-862
    • Lu, Y.1    Yeung, N.2    Sieracki, N.3    Marshall, N.M.4
  • 2
    • 77949860707 scopus 로고    scopus 로고
    • Designing artificial enzymes by intuition and computation
    • Nanda V, Koder RL (2010) Designing artificial enzymes by intuition and computation. Nat Chem 2(1):15-24.
    • (2010) Nat Chem , vol.2 , Issue.1 , pp. 15-24
    • Nanda, V.1    Koder, R.L.2
  • 4
    • 73549117481 scopus 로고    scopus 로고
    • An artificial di-iron oxo-protein with phenol oxidase activity
    • Faiella M, et al. (2009) An artificial di-iron oxo-protein with phenol oxidase activity. Nat Chem Biol 5(12):882-884.
    • (2009) Nat Chem Biol , vol.5 , Issue.12 , pp. 882-884
    • Faiella, M.1
  • 5
    • 84860773275 scopus 로고    scopus 로고
    • Catalysis by a de novo zinc-mediated protein interface: Implications for natural enzyme evolution and rational enzyme engineering
    • Der BS, Edwards DR, Kuhlman B (2012) Catalysis by a de novo zinc-mediated protein interface: Implications for natural enzyme evolution and rational enzyme engineering. Biochemistry 51(18):3933-3940.
    • (2012) Biochemistry , vol.51 , Issue.18 , pp. 3933-3940
    • Der, B.S.1    Edwards, D.R.2    Kuhlman, B.3
  • 6
    • 84856397386 scopus 로고    scopus 로고
    • Hydrolytic catalysis and structural stabilization in a designed metalloprotein
    • Zastrow ML, Peacock AFA, Stuckey JA, Pecoraro VL (2012) Hydrolytic catalysis and structural stabilization in a designed metalloprotein. Nat Chem 4(2):118-123.
    • (2012) Nat Chem , vol.4 , Issue.2 , pp. 118-123
    • Zastrow, M.L.1    Peacock, A.F.A.2    Stuckey, J.A.3    Pecoraro, V.L.4
  • 7
    • 0001076517 scopus 로고    scopus 로고
    • Dissimilatory nitrite and nitric oxide reductases
    • Averill BA (1996) Dissimilatory nitrite and nitric oxide reductases. Chem Rev 96(7):2951-2964.
    • (1996) Chem Rev , vol.96 , Issue.7 , pp. 2951-2964
    • Averill, B.A.1
  • 8
    • 0033788756 scopus 로고    scopus 로고
    • Metal coordination and mechanism of multicopper nitrite reductase
    • Suzuki S, Kataoka K, Yamaguchi K (2000) Metal coordination and mechanism of multicopper nitrite reductase. Acc Chem Res 33(10):728-735.
    • (2000) Acc Chem Res , vol.33 , Issue.10 , pp. 728-735
    • Suzuki, S.1    Kataoka, K.2    Yamaguchi, K.3
  • 10
    • 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
    • DOI 10.1021/bi971603z
    • 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. (Pubitemid 28196765)
    • (1998) Biochemistry , vol.37 , Issue.17 , 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
  • 11
    • 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
  • 14
    • 33846158761 scopus 로고    scopus 로고
    • Incorporating electron-transfer functionality into synthetic metalloproteins from the bottom-up
    • Hong J, Kharenko OA, Ogawa MY (2006) Incorporating electron-transfer functionality into synthetic metalloproteins from the bottom-up. Inorg Chem 45(25):9974-9984.
    • (2006) Inorg Chem , vol.45 , Issue.25 , pp. 9974-9984
    • Hong, J.1    Kharenko, O.A.2    Ogawa, M.Y.3
  • 18
    • 7744232977 scopus 로고    scopus 로고
    • Spectroscopic identification of different types of copper centers generated in synthetic four-helix bundle proteins
    • DOI 10.1021/ja0484294
    • Schnepf R, Haehnel W, Wieghardt K, Hildebrandt P (2004) Spectroscopic identification of different types of copper centers generated in synthetic four-helix bundle proteins. J Am Chem Soc 126(44):14389-14399. (Pubitemid 39463622)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.44 , pp. 14389-14399
    • Schnepf, R.1    Haehnel, W.2    Wieghardt, K.3    Hildebrandt, P.4
  • 19
    • 70350144669 scopus 로고    scopus 로고
    • The effect of the side chain length of Asp and Glu on coordination structure of Cu(2+) in a de novo designed protein
    • Shiga D, et al. (2009) The effect of the side chain length of Asp and Glu on coordination structure of Cu(2+) in a de novo designed protein. Biopolymers 91(11):907-916.
    • (2009) Biopolymers , vol.91 , Issue.11 , pp. 907-916
    • Shiga, D.1
  • 20
    • 2442626744 scopus 로고    scopus 로고
    • Binding of Cu(II) or Zn(II) in a de novo designed triple-stranded α-helical coiled-coil toward a prototype for a metalloenzyme
    • DOI 10.1111/j.1399-3011.2004.00109.x
    • Kiyokawa T, et al. (2004) Binding of Cu(II) or Zn(II) in a de novo designed triple-stranded α-helical coiled-coil toward a prototype for a metalloenzyme. J Pept Res 63(4):347-353. (Pubitemid 38639539)
    • (2004) Journal of Peptide Research , vol.63 , Issue.4 , pp. 347-353
    • Kiyokawa, T.1    Kanaori, K.2    Tajima, K.3    Koike, M.4    Mizuno, T.5    Oku, J.-I.6    Tanaka, T.7
  • 21
    • 33748244071 scopus 로고
    • De novo design of a novel heterodinuclear three-helix bundle metalloprotein
    • Ghadiri MR, Case MA (1993) De novo design of a novel heterodinuclear three-helix bundle metalloprotein. Angew Chem Int Ed Engl 32(11):1594-1597.
    • (1993) Angew Chem Int Ed Engl , vol.32 , Issue.11 , pp. 1594-1597
    • Ghadiri, M.R.1    Case, M.A.2
  • 22
    • 78650604377 scopus 로고    scopus 로고
    • Creation of a type 1 blue copper site within a de novo coiled-coil protein scaffold
    • Shiga D, et al. (2010) Creation of a type 1 blue copper site within a de novo coiled-coil protein scaffold. J Am Chem Soc 132(51):18191-18198.
    • (2010) J Am Chem Soc , vol.132 , Issue.51 , pp. 18191-18198
    • Shiga, D.1
  • 23
    • 84862643055 scopus 로고    scopus 로고
    • Control of enzyme reaction by a designed metal-ion-dependent α-helical coiled-coil protein
    • Murase S, Ishino S, Ishino Y, Tanaka T (2012) Control of enzyme reaction by a designed metal-ion-dependent α-helical coiled-coil protein. J Biol Inorg Chem 17(5):791-799.
    • (2012) J Biol Inorg Chem , vol.17 , Issue.5 , pp. 791-799
    • Murase, S.1    Ishino, S.2    Ishino, Y.3    Tanaka, T.4
  • 24
    • 84867447447 scopus 로고    scopus 로고
    • Creation of a binuclear purple copper site within a de novo coiled-coil protein
    • Shiga D, et al. (2012) Creation of a binuclear purple copper site within a de novo coiled-coil protein. Biochemistry 51(40):7901-7907.
    • (2012) Biochemistry , vol.51 , Issue.40 , pp. 7901-7907
    • Shiga, D.1
  • 25
    • 33846669977 scopus 로고    scopus 로고
    • Ab initio modelling of the structure and redox behaviour of copper(I) bound to a His-His model peptide: Relevance to the β-amyloid peptide of Alzheimer's disease
    • DOI 10.1007/s00775-006-0175-9
    • Raffa DF, Rickard GA, Rauk A (2007) Ab initio modelling of the structure and redox behaviour of copper(I) bound to a His-His model peptide: Relevance to the β-amyloid peptide of Alzheimer's disease. J Biol Inorg Chem 12(2):147-164. (Pubitemid 46197940)
    • (2007) Journal of Biological Inorganic Chemistry , vol.12 , Issue.2 , pp. 147-164
    • Raffa, D.F.1    Rickard, G.A.2    Rauk, A.3
  • 26
    • 33845283452 scopus 로고
    • X-ray absorption edge determination of the oxidation state and coordination number of copper. Application to the type 3 site in Rhus vernicifera laccase and its reaction with oxygen
    • Kau LS, Spira-Solomon DJ, Penner-Hahn JE, Hodgson KO, Solomon EI (1987) X-ray absorption edge determination of the oxidation state and coordination number of copper. Application to the type 3 site in Rhus vernicifera laccase and its reaction with oxygen. J Am Chem Soc 109(21):6433-6442.
    • (1987) J Am Chem Soc , vol.109 , Issue.21 , pp. 6433-6442
    • Kau, L.S.1    Spira-Solomon, D.J.2    Penner-Hahn, J.E.3    Hodgson, K.O.4    Solomon, E.I.5
  • 27
    • 0141888996 scopus 로고    scopus 로고
    • 2 center constitutes the high-affinity metal-sensing site in the CueR metalloregulatory protein
    • DOI 10.1021/ja036070y
    • Chen K, Yuldasheva S, Penner-Hahn JE, O'Halloran TV (2003) An atypical linear Cu(I)-S2 center constitutes the high-affinity metal-sensing site in the CueR metalloregulatory protein. J Am Chem Soc 125(40):12088-12089. (Pubitemid 37238832)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.40 , pp. 12088-12089
    • Chen, K.1    Yuldasheva, S.2    Penner-Hahn, J.E.3    O'Halloran, T.V.4
  • 28
    • 0037095428 scopus 로고    scopus 로고
    • Group-fitted ab initiosingle- and multiple-scattering EXAFS Debye-Waller factors
    • Dimakis N, Bunker G (2002) Group-fitted ab initiosingle- and multiple-scattering EXAFS Debye-Waller factors. Phys Rev B Condens Matter 65(20):201103.
    • (2002) Phys Rev B Condens Matter , vol.65 , Issue.20 , pp. 201103
    • Dimakis, N.1    Bunker, G.2
  • 29
    • 0000607756 scopus 로고    scopus 로고
    • Spectrum-structure correlation for visible absorption spectra of copper(II) complexes in aqueous solution
    • Prenesti E, Daniele PG, Prencipe M, Ostacoli G (1999) Spectrum-structure correlation for visible absorption spectra of copper(II) complexes in aqueous solution. Polyhedron 18(25):3233- 3241.
    • (1999) Polyhedron , vol.18 , Issue.25 , pp. 3233-3241
    • Prenesti, E.1    Daniele, P.G.2    Prencipe, M.3    Ostacoli, G.4
  • 30
    • 33846350883 scopus 로고    scopus 로고
    • Electronic structure of the two copper sites in nitrite reductase by 9 and 95 GHz EPR on cavity mutants
    • Fittipaldi M, Wijma HJ, Verbeet MP, Canters GW, Huber M (2006) Electronic structure of the two copper sites in nitrite reductase by 9 and 95 GHz EPR on cavity mutants. Appl Magn Reson 30(3):417-426.
    • (2006) Appl Magn Reson , vol.30 , Issue.3 , pp. 417-426
    • Fittipaldi, M.1    Wijma, H.J.2    Verbeet, M.P.3    Canters, G.W.4    Huber, M.5
  • 31
    • 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
    • DOI 10.1021/ja075575b
    • 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. (Pubitemid 351657285)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.19 , pp. 6088-6098
    • Kujime, M.1    Izumi, C.2    Tomura, M.3    Hada, M.4    Fujii, H.5
  • 32
    • 33645548530 scopus 로고    scopus 로고
    • (N-Benzyl-bis-N′,N″-salicylidene)-cis-1,3, 5-triaminocyclohexane copper(II): A novel catalyst for the aerobic oxidation of benzyl alcohol
    • Nairn AK, et al. (2006) (N-Benzyl-bis-N′,N″-salicylidene)- cis-1,3,5-triaminocyclohexane copper(II): A novel catalyst for the aerobic oxidation of benzyl alcohol. Dalton Trans (1):172-176.
    • (2006) Dalton Trans , Issue.1 , pp. 172-176
    • Nairn, A.K.1
  • 33
    • 1642404510 scopus 로고    scopus 로고
    • C-Terminal Domain of the Membrane Copper Transporter Ctr1 from Saccharomyces cerevisiae Binds Four Cu(I) Ions as a Cuprous-Thiolate Polynuclear Cluster: Sub-femtomolar Cu(I) Affinity of Three Proteins Involved in Copper Trafficking
    • DOI 10.1021/ja0390350
    • Xiao Z, Loughlin F, George GN, Howlett GJ, Wedd AG (2004) C-terminal domain of the membrane copper transporter Ctr1 from Saccharomyces cerevisiae binds four Cu(I) ions as a cuprous-thiolate polynuclear cluster: Sub-femtomolar Cu(I) affinity of three proteins involved in copper trafficking. J Am Chem Soc 126(10):3081-3090. (Pubitemid 38380713)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.10 , pp. 3081-3090
    • Xiao, Z.1    Loughlin, F.2    George, G.N.3    Howlett, G.J.4    Wedd, A.G.5
  • 35
    • 33645548612 scopus 로고    scopus 로고
    • Using synthetic chemistry to understand copper protein active sites: A personal perspective
    • Tolman WB (2006) Using synthetic chemistry to understand copper protein active sites: A personal perspective. J Biol Inorg Chem 11(3):261-271.
    • (2006) J Biol Inorg Chem , vol.11 , Issue.3 , pp. 261-271
    • Tolman, W.B.1
  • 36
    • 0036105395 scopus 로고    scopus 로고
    • Copper complexes with N-donor ligands as models of the active centres of nitrite reductase and related enzymes
    • 2002
    • Richards RL, Durrant MC (2002) Copper complexes with N-donor ligands as models of the active centres of nitrite reductase and related enzymes. J Chem Res 2002(3):95-98.
    • (2002) J Chem Res , Issue.3 , pp. 95-98
    • Richards, R.L.1    Durrant, M.C.2
  • 37
    • 79953041532 scopus 로고    scopus 로고
    • Model peptides provide new insights into the role of histidine residues as potential ligands in human cellular copper acquisition via Ctr1
    • Haas KL, Putterman AB, White DR, Thiele DJ, Franz KJ (2011) Model peptides provide new insights into the role of histidine residues as potential ligands in human cellular copper acquisition via Ctr1. J Am Chem Soc 133(12):4427-4437.
    • (2011) J Am Chem Soc , vol.133 , Issue.12 , pp. 4427-4437
    • Haas, K.L.1    Putterman, A.B.2    White, D.R.3    Thiele, D.J.4    Franz, K.J.5
  • 38
    • 84855375181 scopus 로고    scopus 로고
    • Reevaluation of copper(I) affinity for amyloid-β peptides by competition with ferrozine - An unusual copper(I) indicator
    • Alies B, Badei B, Faller P, Hureau C (2012) Reevaluation of copper(I) affinity for amyloid-β peptides by competition with ferrozine - an unusual copper(I) indicator. Chemistry 18(4):1161-1167.
    • (2012) Chemistry , vol.18 , Issue.4 , pp. 1161-1167
    • Alies, B.1    Badei, B.2    Faller, P.3    Hureau, C.4
  • 40
    • 0034123872 scopus 로고    scopus 로고
    • Major changes in copper coordination accompany reduction of peptidylglycine monooxygenase: Implications for electron transfer and the catalytic mechanism
    • Blackburn NJ, Rhames FC, Ralle M, Jaron S (2000) Major changes in copper coordination accompany reduction of peptidylglycine monooxygenase: Implications for electron transfer and the catalytic mechanism. J Biol Inorg Chem 5(3):341-353. (Pubitemid 30407893)
    • (2000) Journal of Biological Inorganic Chemistry , vol.5 , Issue.3 , pp. 341-353
    • Blackburn, N.J.1    Rhames, F.C.2    Ralle, M.3    Jaron, S.4
  • 41
    • 0038203241 scopus 로고    scopus 로고
    • Oxygen activation in a copper-containing amine oxidase
    • Wilmot CM (2003) Oxygen activation in a copper-containing amine oxidase. Biochem Soc Trans 31(Pt 3):493-496.
    • (2003) Biochem Soc Trans , vol.31 , Issue.PART 3 , pp. 493-496
    • Wilmot, C.M.1
  • 42
    • 0026701748 scopus 로고
    • Evidence that the type 2 copper centers are the site of nitrite reduction by Achromobacter cycloclastes nitrite reductase
    • Libby E, Averill BA (1992) Evidence that the type 2 copper centers are the site of nitrite reduction by Achromobacter cycloclastes nitrite reductase. Biochem Biophys Res Commun 187(3):1529-1535.
    • (1992) Biochem Biophys Res Commun , vol.187 , Issue.3 , pp. 1529-1535
    • Libby, E.1    Averill, B.A.2
  • 43
    • 65249168774 scopus 로고    scopus 로고
    • Thermodynamic equilibrium between blue and green copper sites and the role of the protein in controlling function
    • Ghosh S, et al. (2009) Thermodynamic equilibrium between blue and green copper sites and the role of the protein in controlling function. Proc Natl Acad Sci USA 106(13):4969-4974.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.13 , pp. 4969-4974
    • Ghosh, S.1
  • 45
    • 0015010707 scopus 로고
    • The electron-accepting sites in Rhus vernicifera laccase as studied by anaerobic oxidation-reduction titrations
    • Reinhammar BRM, Vänngård TI (1971) The electron-accepting sites in Rhus vernicifera laccase as studied by anaerobic oxidation-reduction titrations. Eur J Biochem 18(4):463-468.
    • (1971) Eur J Biochem , vol.18 , Issue.4 , pp. 463-468
    • Reinhammar, B.R.M.1    Vänngård, T.I.2
  • 46
    • 33745238976 scopus 로고    scopus 로고
    • A random-sequential mechanism for nitrite binding and active site reduction in copper-containing nitrite reductase
    • Wijma HJ, Jeuken LJC, Verbeet MP, Armstrong FA, Canters GW (2006) A random-sequential 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.C.2    Verbeet, M.P.3    Armstrong, F.A.4    Canters, G.W.5
  • 47
    • 74449084550 scopus 로고    scopus 로고
    • Electroreduction of nitrite to nitrogen oxide by a copper-containing nitrite reductase model complex incorporated into collagen film
    • Isoda N, Yokoyama H, Nojiri M, Suzuki S, Yamaguchi K (2010) Electroreduction of nitrite to nitrogen oxide by a copper-containing nitrite reductase model complex incorporated into collagen film. Bioelectrochemistry 77(2):82-88.
    • (2010) Bioelectrochemistry , vol.77 , Issue.2 , pp. 82-88
    • Isoda, N.1    Yokoyama, H.2    Nojiri, M.3    Suzuki, S.4    Yamaguchi, K.5
  • 48
    • 0000263553 scopus 로고
    • Molecular structure of nitro- and nitrito-copper complexes as reaction intermediates in electrochemical reduction of nitrite to dinitrogen oxide
    • Komeda N, et al. (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(2):581-589.
    • (1995) Bull Chem Soc Jpn , vol.68 , Issue.2 , pp. 581-589
    • Komeda, N.1
  • 49
    • 33746323645 scopus 로고    scopus 로고
    • Spectroscopic characterization of reaction intermediates in a model for copper nitrite reductase
    • DOI 10.1002/anie.200503555
    • Kujime M, Fujii H (2006) Spectroscopic characterization of reaction intermediates in a model for copper nitrite reductase. Angew Chem Int Ed Engl 45(7):1089-1092. (Pubitemid 44104893)
    • (2006) Angewandte Chemie - International Edition , vol.45 , Issue.7 , pp. 1089-1092
    • Kujime, M.1    Fujii, H.2
  • 51
    • 26444544297 scopus 로고    scopus 로고
    • Electroreduction of nitrite on gold electrode modified with Cu-containing nitrite reductase model complex
    • DOI 10.1039/b507932b
    • Hiratsu T, Suzuki S, Yamaguchi K (2005) Electroreduction of nitrite on gold electrode modified with Cu-containing nitrite reductase model complex. Chem Commun (Camb) (36):4534-4535. (Pubitemid 41430465)
    • (2005) Chemical Communications , Issue.36 , pp. 4534-4535
    • Hiratsu, T.1    Suzuki, S.2    Yamaguchi, K.3
  • 52
    • 33748613775 scopus 로고    scopus 로고
    • Photochemical reduction of nitrite catalyzed by a Cu-containing nitrite reductase model complex and a photosensitizer under irradiation with visible light
    • Yamaguchi K, Okada T, Suzuki S (2006) Photochemical reduction of nitrite catalyzed by a Cu-containing nitrite reductase model complex and a photosensitizer under irradiation with visible light. Inorg Chem Commun 9(10):989-991.
    • (2006) Inorg Chem Commun , vol.9 , Issue.10 , pp. 989-991
    • Yamaguchi, K.1    Okada, T.2    Suzuki, S.3
  • 53
    • 71449097806 scopus 로고    scopus 로고
    • Electrocatalytic nitrite reduction to nitrogen oxide by a synthetic analogue of the active site of Cu-containing nitrite reductase incorporated in Nafion film
    • Migita Y, et al. (2009) Electrocatalytic nitrite reduction to nitrogen oxide by a synthetic analogue of the active site of Cu-containing nitrite reductase incorporated in Nafion film. Electroanalysis 21(22):2441-2446.
    • (2009) Electroanalysis , vol.21 , Issue.22 , pp. 2441-2446
    • Migita, Y.1
  • 54
    • 0001333656 scopus 로고    scopus 로고
    • Structural and Electrochemical Comparison of Copper(II) Complexes with Tripodal Ligands
    • Nagao H, Komeda N, Mukaida M, Suzuki M, Tanaka K (1996) Structural and electrochemical comparison of copper(II) complexes with tripodal ligands. Inorg Chem 35(23):6809-6815. (Pubitemid 126453103)
    • (1996) Inorganic Chemistry , vol.35 , Issue.23 , pp. 6809-6815
    • Nagao, H.1    Komeda, N.2    Mukaida, M.3    Suzuki, M.4    Tanaka, K.5
  • 56
    • 0035807939 scopus 로고    scopus 로고
    • Thermodynamic model for the stabilization of trigonal thiolato mercury(II) in designed three-stranded coiled coils
    • DOI 10.1021/bi015649a
    • Farrer BT, Harris NP, Balchus KE, Pecoraro VL (2001) Thermodynamic model for the stabilization of trigonal thiolato mercury(II) in designed three-stranded coiled coils. Biochemistry 40(48):14696-14705. (Pubitemid 33111754)
    • (2001) Biochemistry , vol.40 , Issue.48 , pp. 14696-14705
    • Farrer, B.T.1    Harris, N.P.2    Balchus, K.E.3    Pecoraro, V.L.4
  • 57
    • 0003795626 scopus 로고    scopus 로고
    • SSRL, Stanford University, USA. Available at
    • George GN (2000) EXAFSPAK. SSRL, Stanford University, USA. Available at http://ssrl. slac.stanford.edu/exafspak.html.
    • (2000) EXAFSPAK
    • George, G.N.1
  • 58
    • 0642303383 scopus 로고    scopus 로고
    • Relativistic calculations of spin-dependent x-ray-absorption spectra
    • Ankudinov AL, Rehr JJ (1997) Relativistic calculations of spin-dependent x-ray-absorption spectra. Phys Rev B Condens Matter 56(4):R1712-R1716.
    • (1997) Phys Rev B Condens Matter , vol.56 , Issue.4
    • Ankudinov, A.L.1    Rehr, J.J.2
  • 60
    • 0000970424 scopus 로고
    • Infrared absorption intensities for N2O
    • Kagann RH (1982) Infrared absorption intensities for N2O. J Mol Spectrosc 95(2):297-305.
    • (1982) J Mol Spectrosc , vol.95 , Issue.2 , pp. 297-305
    • Kagann, R.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.