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Volumn 40, Issue 7, 2007, Pages 563-572

Heme-copper/dioxygen adduct formation, properties, and reactivity

Author keywords

[No Author keywords available]

Indexed keywords

COPPER; CYTOCHROME C OXIDASE; FERRIC ION; HEME; IMIDAZOLE DERIVATIVE; LIGAND; OXYGEN; PHENOL DERIVATIVE;

EID: 34547774772     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar700031t     Document Type: Conference Paper
Times cited : (130)

References (48)
  • 1
    • 33645866880 scopus 로고    scopus 로고
    • 2nd ed, King, R. B, Ed, John Wiley and Sons Ltd, New York
    • Walker, F. A.; Simonis, U. In Encyclopedia of Inorganic Chemistry, 2nd ed.; King, R. B., Ed.; John Wiley and Sons Ltd.: New York, 2005; Vol. 4, pp 2390-2521.
    • (2005) Encyclopedia of Inorganic Chemistry , vol.4 , pp. 2390-2521
    • Walker, F.A.1    Simonis, U.2
  • 2
    • 33645224224 scopus 로고    scopus 로고
    • Mononuclear copper active-oxygen complexes
    • Itoh, S. Mononuclear copper active-oxygen complexes. Curr. Opin. Chem. Biol. 2006, 10, 115-122.
    • (2006) Curr. Opin. Chem. Biol , vol.10 , pp. 115-122
    • Itoh, S.1
  • 4
    • 1542304579 scopus 로고    scopus 로고
    • Structure and spectroscopy of copper-dioxygen complexes
    • Mirica, L. M.; Ottenwaelder, X.; Stack, T. D. P. Structure and spectroscopy of copper-dioxygen complexes. Chem. Rev. 2004, 104, 1013-1045.
    • (2004) Chem. Rev , vol.104 , pp. 1013-1045
    • Mirica, L.M.1    Ottenwaelder, X.2    Stack, T.D.P.3
  • 5
    • 1542288709 scopus 로고    scopus 로고
    • Reactivity of dioxygen-copper systems
    • Lewis, E. A.; Tolman, W. B. Reactivity of dioxygen-copper systems. Chem. Rev. 2004, 104, 1047-1076.
    • (2004) Chem. Rev , vol.104 , pp. 1047-1076
    • Lewis, E.A.1    Tolman, W.B.2
  • 6
    • 1542288700 scopus 로고    scopus 로고
    • Synthetic models for heme-copper oxidases
    • Kim, E.; Chufán, E. E.; Kamaraj, K.; Karlin, K. D. Synthetic models for heme-copper oxidases. Chem. Rev. 2004, 104, 1077-1133.
    • (2004) Chem. Rev , vol.104 , pp. 1077-1133
    • Kim, E.1    Chufán, E.E.2    Kamaraj, K.3    Karlin, K.D.4
  • 7
    • 1542334754 scopus 로고    scopus 로고
    • Functional analogues of cytochrome c oxidase, myoglobin, and hemoglobin
    • Collman, J. P.; Boulatov, R.; Sunderland, C. J.; Fu, L. Functional analogues of cytochrome c oxidase, myoglobin, and hemoglobin. Chem. Rev. 2004, 104, 561-588.
    • (2004) Chem. Rev , vol.104 , pp. 561-588
    • Collman, J.P.1    Boulatov, R.2    Sunderland, C.J.3    Fu, L.4
  • 11
    • 16244423655 scopus 로고    scopus 로고
    • Dioxygen activation by copper, heme and non-heme iron enzymes: Comparison of electronic structures and reactivities
    • Decker, A.; Solomon, E. I. Dioxygen activation by copper, heme and non-heme iron enzymes: Comparison of electronic structures and reactivities. Curr. Opin. Chem. Biol. 2005, 9, 152-163.
    • (2005) Curr. Opin. Chem. Biol , vol.9 , pp. 152-163
    • Decker, A.1    Solomon, E.I.2
  • 12
    • 33748898492 scopus 로고    scopus 로고
    • Different types of biological proton transfer reactions studied by quantum chemical methods
    • Blomberg, M. R. A.; Siegbahn, P. E. M. Different types of biological proton transfer reactions studied by quantum chemical methods. Biochim. Biophys. Acta 2006, 1757, 969-980.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 969-980
    • Blomberg, M.R.A.1    Siegbahn, P.E.M.2
  • 13
    • 33749413911 scopus 로고
    • Synthetic approach to the structure and function of copper proteins
    • Kitajima, N. Synthetic approach to the structure and function of copper proteins. Adv. Inorg. Chem. 1992, 39, 1-77.
    • (1992) Adv. Inorg. Chem , vol.39 , pp. 1-77
    • Kitajima, N.1
  • 14
    • 0642345300 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of copper(I)/dioxygen interaction
    • Karlin, K. D.; Kaderli, S.; Zuberbühler, A. D. Kinetics and thermodynamics of copper(I)/dioxygen interaction. Acc. Chem. Res. 1997, 30, 139-147.
    • (1997) Acc. Chem. Res , vol.30 , pp. 139-147
    • Karlin, K.D.1    Kaderli, S.2    Zuberbühler, A.D.3
  • 16
    • 34547763951 scopus 로고    scopus 로고
    • -.
    • -.
  • 17
    • 0001068249 scopus 로고
    • II] bridge: An analogue of the binuclear site in oxidized cytochrome coxidase
    • II] bridge: An analogue of the binuclear site in oxidized cytochrome coxidase. J. Am. Chem. Soc. 1993, 115, 11789-11798.
    • (1993) J. Am. Chem. Soc , vol.115 , pp. 11789-11798
    • Lee, S.C.1    Holm, R.H.2
  • 19
    • 0030038165 scopus 로고    scopus 로고
    • XAS structural comparisons and reversibly interconvertible oxo and hydroxo bridged heme-copper oxidase model compounds
    • Fox, S.; Nanthakumar, A.; Wikström, M.; Karlin, K. D.; Blackburn, N. J. XAS structural comparisons and reversibly interconvertible oxo and hydroxo bridged heme-copper oxidase model compounds. J. Am. Chem. Soc. 1996, 118, 24-34.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 24-34
    • Fox, S.1    Nanthakumar, A.2    Wikström, M.3    Karlin, K.D.4    Blackburn, N.J.5
  • 20
    • 85050238274 scopus 로고
    • Slow proton-transfer reactions in organometallic and bioinorganic chemistry
    • Kramarz, K. W.; Norton, J. R. Slow proton-transfer reactions in organometallic and bioinorganic chemistry. Prog. Inorg. Chem. 1994, 42, 1-65.
    • (1994) Prog. Inorg. Chem , vol.42 , pp. 1-65
    • Kramarz, K.W.1    Norton, J.R.2
  • 21
    • 12144288091 scopus 로고    scopus 로고
    • Ghiladi, R. A.; Ju, T. D.; Lee, D.-H.; Moënne-Loccoz, P.; Kaderli, S.; Neuhold, Y.-M.; Zuberbühler, A. D.; Woods, A. S.; Cotter, R. J.; Karlin, K. D. Formation and characterization of a high-spin heme-copper dioxygen (peroxo) complex. J. Am. Chem. Soc. 1999, 121, 9885-9886.
    • Ghiladi, R. A.; Ju, T. D.; Lee, D.-H.; Moënne-Loccoz, P.; Kaderli, S.; Neuhold, Y.-M.; Zuberbühler, A. D.; Woods, A. S.; Cotter, R. J.; Karlin, K. D. Formation and characterization of a high-spin heme-copper dioxygen (peroxo) complex. J. Am. Chem. Soc. 1999, 121, 9885-9886.
  • 23
    • 0032365990 scopus 로고    scopus 로고
    • II complex. A modeling reaction of the heme-Cu site in cytochrome coxidase
    • II complex. A modeling reaction of the heme-Cu site in cytochrome coxidase. Chem. Lett. 1998, 351-352.
    • (1998) Chem. Lett , pp. 351-352
    • Sasaki, T.1    Nakamura, N.2    Naruta, Y.3
  • 25
    • 0347695004 scopus 로고    scopus 로고
    • An iron-peroxo porphyrin complex. New synthesis and nucleophilic reactivity toward a Cu(II) complex giving a heme-peroxo-copper adduct
    • Chufán, E. E.; Karlin, K. D. An iron-peroxo porphyrin complex. New synthesis and nucleophilic reactivity toward a Cu(II) complex giving a heme-peroxo-copper adduct. J. Am. Chem. Soc. 2003, 125, 16160-16161.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 16160-16161
    • Chufán, E.E.1    Karlin, K.D.2
  • 27
    • 34547802880 scopus 로고    scopus 로고
    • Complex, F8FeIII-(O2 2, CuII(TMPA, 1) was also investigated using 676 nm excitation; the νO-O (now observed at 810 cm-1) and two different M-O vibrations at 533 and 511 cm -1 were clearly identified. Normal coordinate analysis and DFT calculations further support that the 810 cm-1 mode is a dominant (80 , O-O stretching vibration, whereas the 533 and 511 cm-1 modes correspond essentially to the νFe-O (where O is the oxygen only bound to Fe; see the structure description of 1, below) and to an asymmetric νas(Fe-O-Cu) vibration, respectively. See ref 28
    • as(Fe-O-Cu) vibration, respectively. See ref 28.
  • 28
    • 34249736263 scopus 로고    scopus 로고
    • +. Inorg. Chem. 2007, 46, 3889-3902.
    • +. Inorg. Chem. 2007, 46, 3889-3902.
  • 29
    • 0035813243 scopus 로고    scopus 로고
    • 2-reduction and ferryl formation. Inorg. Chem. 2001, 40, 5754-5767.
    • 2-reduction and ferryl formation. Inorg. Chem. 2001, 40, 5754-5767.
  • 30
    • 0037384039 scopus 로고    scopus 로고
    • 2 reactivity studies: Copper-ligand influences in cytochrome coxidase models. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 3623-3628.
    • 2 reactivity studies: Copper-ligand influences in cytochrome coxidase models. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 3623-3628.
  • 31
    • 33846213208 scopus 로고    scopus 로고
    • Maiti, D.; Fry, H. C.; Woertink, J. S.; Vance, M. A.; Solomon, E. I.; Karlin, K. D. A 1:1 copper-dioxygen adduct is an end-on bound superoxo copper(II) complex which undergoes oxygenation reactions with phenols. J. Am. Chem. Soc. 2007, 129, 264-265.
    • Maiti, D.; Fry, H. C.; Woertink, J. S.; Vance, M. A.; Solomon, E. I.; Karlin, K. D. A 1:1 copper-dioxygen adduct is an end-on bound superoxo copper(II) complex which undergoes oxygenation reactions with phenols. J. Am. Chem. Soc. 2007, 129, 264-265.
  • 32
    • 0002889337 scopus 로고    scopus 로고
    • Nucleophilicity of iron-peroxo porphyrin complexes
    • Wertz, D. L.; Valentine, J. S. Nucleophilicity of iron-peroxo porphyrin complexes. Struct. Bonding 2000, 97, 37-60.
    • (2000) Struct. Bonding , vol.97 , pp. 37-60
    • Wertz, D.L.1    Valentine, J.S.2
  • 36
    • 0000941098 scopus 로고
    • Spectroscopic and theoretical studies of an end-on peroxide-bridged coupled binuclear copper(II) model complex of relevance to the active sites in hemocyanin and tyrosinase
    • Baldwin, M. J.; Ross, P. K.; Pate, J. E.; Tyeklar, Z.; Karlin, K. D.; Solomon, E. I. Spectroscopic and theoretical studies of an end-on peroxide-bridged coupled binuclear copper(II) model complex of relevance to the active sites in hemocyanin and tyrosinase. J. Am. Chem. Soc. 1991, 113, 8671-8679.
    • (1991) J. Am. Chem. Soc , vol.113 , pp. 8671-8679
    • Baldwin, M.J.1    Ross, P.K.2    Pate, J.E.3    Tyeklar, Z.4    Karlin, K.D.5    Solomon, E.I.6
  • 37
    • 0029970639 scopus 로고    scopus 로고
    • The diverse reactivity of peroxy ferric porphyrin complexes of electron-rich and electron-poor porphyrins
    • Selke, M.; Sisemore, M. F.; Valentine, J. S. The diverse reactivity of peroxy ferric porphyrin complexes of electron-rich and electron-poor porphyrins. J. Am. Chem. Soc. 1996, 118, 2008-2012.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 2008-2012
    • Selke, M.1    Sisemore, M.F.2    Valentine, J.S.3
  • 38
    • 34547771827 scopus 로고    scopus 로고
    • + (1), with the latter possessing the expected orbital energy ordering for high-spin iron(III).
    • + (1), with the latter possessing the expected orbital energy ordering for high-spin iron(III).
  • 39
    • 26944487641 scopus 로고    scopus 로고
    • Tridentate copper ligand influences on heme-peroxo-copper formation and properties: Reduced, superoxo, and μ-peroxo iron/copper complexes
    • Kim, E.; Helton, M. E.; Lu, S.; Moënne-Loccoz, P.; Incarvito, C. D.; Rheingold, A. L.; Kaderli, S.; Zuberbühler, A. D.; Karlin, K. D. Tridentate copper ligand influences on heme-peroxo-copper formation and properties: Reduced, superoxo, and μ-peroxo iron/copper complexes. Inorg, Chem. 2005, 44, 7014-7029.
    • (2005) Inorg, Chem , vol.44 , pp. 7014-7029
    • Kim, E.1    Helton, M.E.2    Lu, S.3    Moënne-Loccoz, P.4    Incarvito, C.D.5    Rheingold, A.L.6    Kaderli, S.7    Zuberbühler, A.D.8    Karlin, K.D.9
  • 40
    • 0000258783 scopus 로고
    • Spectroscopy of binuclear dioxygen complexes
    • Solomon, E. I.; Tuczek, F.; Root, D. E.; Brown, C. A. Spectroscopy of binuclear dioxygen complexes. Chem. Rev. 1994, 94, 827-856.
    • (1994) Chem. Rev , vol.94 , pp. 827-856
    • Solomon, E.I.1    Tuczek, F.2    Root, D.E.3    Brown, C.A.4
  • 41
    • 0038209163 scopus 로고    scopus 로고
    • Spectroscopic evidence for a heme-superoxide/Cu(I) intermediate in a functional model of cytochrome coxidase
    • Collman, J. P.; Sunderland, C. J.; Berg, K. E.; Vance, M. A.; Solomon, E. I. Spectroscopic evidence for a heme-superoxide/Cu(I) intermediate in a functional model of cytochrome coxidase. J. Am. Chem. Soc. 2003, 125, 6648-6649.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 6648-6649
    • Collman, J.P.1    Sunderland, C.J.2    Berg, K.E.3    Vance, M.A.4    Solomon, E.I.5
  • 43
    • 0038288919 scopus 로고    scopus 로고
    • Copper(I) and copper(II) complexes possessing cross-linked imidazole-phenol ligands: Structures and dioxygen reactivity
    • Kamaraj, K.; Kim, E.; Galliker, B.; Zakharov, L. N.; Rheingold, A. L.; Zuberbuehler, A. D.; Karlin, K. D. Copper(I) and copper(II) complexes possessing cross-linked imidazole-phenol ligands: Structures and dioxygen reactivity. J. Am. Chem. Soc. 2003, 125, 6028-6029.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 6028-6029
    • Kamaraj, K.1    Kim, E.2    Galliker, B.3    Zakharov, L.N.4    Rheingold, A.L.5    Zuberbuehler, A.D.6    Karlin, K.D.7
  • 45
    • 33750989351 scopus 로고    scopus 로고
    • B site of cytochrome c oxidase: Steady-state and transient absorption measurements, UV resonance Raman spectroscopy, EPR spectroscopy, and DFT calculations for M-BIAIP
    • B site of cytochrome c oxidase: Steady-state and transient absorption measurements, UV resonance Raman spectroscopy, EPR spectroscopy, and DFT calculations for M-BIAIP. J. Am. Chem. Soc. 2006, 128, 14560-14570.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 14560-14570
    • Nagano, Y.1    Liu, J.G.2    Naruta, Y.3    Ikoma, T.4    Tero-Kubota, S.5    Kitagawa, T.6
  • 47
    • 32344448823 scopus 로고    scopus 로고
    • The role of tryptophan 272 in the Paracoccus denitrificans cytochrome c oxidase
    • MacMillan, F.; Budiman, K.; Angerer, H.; Michel, H. The role of tryptophan 272 in the Paracoccus denitrificans cytochrome c oxidase. FEBS Lett. 2006, 580, 1345-1349.
    • (2006) FEBS Lett , vol.580 , pp. 1345-1349
    • MacMillan, F.1    Budiman, K.2    Angerer, H.3    Michel, H.4
  • 48
    • 34547746486 scopus 로고    scopus 로고
    • Puiu, S. C.; Chufan, E. E.; Mondal, B.; Karlin, K. D. Heme/Cu complexes as functional models for the active site of cytochrome c oxidase. Abstracts of Papers, 230th ACS National Meeting, Washington, D.C., Aug 28-Sept 1, 2005, 230, U2157-U2158, INOR-307.
    • Puiu, S. C.; Chufan, E. E.; Mondal, B.; Karlin, K. D. Heme/Cu complexes as functional models for the active site of cytochrome c oxidase. Abstracts of Papers, 230th ACS National Meeting, Washington, D.C., Aug 28-Sept 1, 2005, 230, U2157-U2158, INOR-307.


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