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Volumn 1411, Issue 2-3, 1999, Pages 310-322

The reactions of copper proteins with nitric oxide

Author keywords

Copper; Cytochrome c oxidase; EPR; Inhibition; Nitric oxide; Oxidase; Rapid reaction

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING); ASCORBATE OXIDASE; CERULOPLASMIN; COPPER ZINC SUPEROXIDE DISMUTASE; CYTOCHROME C OXIDASE; GALACTOSE OXIDASE; HEMOCYANIN; LACCASE; MONOPHENOL MONOOXYGENASE; NITRIC OXIDE; OXIDOREDUCTASE;

EID: 0032899131     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2728(99)00022-5     Document Type: Review
Times cited : (51)

References (60)
  • 1
    • 0028917372 scopus 로고
    • Nitric oxide signaling in the central nervous system
    • Garthwaite J., Boulton C.L. Nitric oxide signaling in the central nervous system. Annu. Rev. Physiol. 57:1995;683-706.
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 683-706
    • Garthwaite, J.1    Boulton, C.L.2
  • 2
    • 0027752805 scopus 로고
    • The L-arginine nitric oxide pathway
    • Moncada S., Higgs A. The L-arginine nitric oxide pathway. New Engl. J. Med. 329:1993;2002-2012.
    • (1993) New Engl. J. Med. , vol.329 , pp. 2002-2012
    • Moncada, S.1    Higgs, A.2
  • 4
    • 7744232873 scopus 로고
    • Monomer and magnetic dipole-coupled Cu2+ EPR signals in nitrosylhemocyanin
    • Schoot Uiterkamp A.J.M. Monomer and magnetic dipole-coupled Cu2+ EPR signals in nitrosylhemocyanin. FEBS Lett. 20:1972;93-96.
    • (1972) FEBS Lett. , vol.20 , pp. 93-96
    • Schoot Uiterkamp, A.J.M.1
  • 5
    • 0015609087 scopus 로고
    • Magnetic dipole-coupled Cu2+ pairs in nitric oxide treated tyrosinase: A structural relationship between the active sites of tyrosinase and hemocyanin
    • Schoot Uiterkamp A.J.M., Mason H.S. Magnetic dipole-coupled Cu2+ pairs in nitric oxide treated tyrosinase: a structural relationship between the active sites of tyrosinase and hemocyanin. Proc. Natl. Acad. Sci. USA. 70:1973;993-996.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 993-996
    • Schoot Uiterkamp, A.J.M.1    Mason, H.S.2
  • 6
    • 0017407059 scopus 로고
    • Nitrite and nitric oxide treatment of Helix pomatia hemocyanin single and double oxidation of the active site
    • Van der Deen H., Hoving H. Nitrite and nitric oxide treatment of Helix pomatia hemocyanin single and double oxidation of the active site. Biochemistry. 16:1977;3519-3525.
    • (1977) Biochemistry , vol.16 , pp. 3519-3525
    • Van Der Deen, H.1    Hoving, H.2
  • 7
    • 0018779772 scopus 로고
    • The reaction of nitrogen monoxide and of nitrite with deoxyhemcyanin and methaemocyanin of Helix pomatia
    • Verplaetse J., Van Tornout P., Defreyn G., Witters R., Lontie R. The reaction of nitrogen monoxide and of nitrite with deoxyhemcyanin and methaemocyanin of Helix pomatia. Eur. J. Biochem. 95:1979;327-331.
    • (1979) Eur. J. Biochem. , vol.95 , pp. 327-331
    • Verplaetse, J.1    Van Tornout, P.2    Defreyn, G.3    Witters, R.4    Lontie, R.5
  • 9
    • 0023645836 scopus 로고
    • The reaction of nitric oxide with copper proteins and the photodissociation of copper-nitric oxide complexes
    • Gorren A.C.F., De Boer E., Wever R. The reaction of nitric oxide with copper proteins and the photodissociation of copper-nitric oxide complexes. Biochim. Biophys. Acta. 916:1987;38-47.
    • (1987) Biochim. Biophys. Acta , vol.916 , pp. 38-47
    • Gorren, A.C.F.1    De Boer, E.2    Wever, R.3
  • 11
    • 0018499136 scopus 로고
    • Structure of cytochrome a3-Cua3 couple in cytochrome c oxidase as revealed by nitric oxide binding studies
    • Stevens T.H., Brudwig G.W., Bocian D.F., Chan S.I. Structure of cytochrome a3-Cua3 couple in cytochrome c oxidase as revealed by nitric oxide binding studies. Proc. Natl. Acad. Sci. USA. 76:1979;3320-3325.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 3320-3325
    • Stevens, T.H.1    Brudwig, G.W.2    Bocian, D.F.3    Chan, S.I.4
  • 12
    • 0019322671 scopus 로고
    • Reactions of nitric oxide with cytochrome c oxidase
    • Brudvig G.W., Stevens T.H., Chan S.I. Reactions of nitric oxide with cytochrome c oxidase. Biochemistry. 19:1980;5275-5285.
    • (1980) Biochemistry , vol.19 , pp. 5275-5285
    • Brudvig, G.W.1    Stevens, T.H.2    Chan, S.I.3
  • 13
    • 0020487171 scopus 로고
    • EPR studies of the photodissociation reactions of cytochrome c oxidase-nitric oxide complexes
    • Boelens R., Rademaker H., Pel R., Wever R. EPR studies of the photodissociation reactions of cytochrome c oxidase-nitric oxide complexes. Biochim. Biophys. Acta. 679:1982;84-94.
    • (1982) Biochim. Biophys. Acta , vol.679 , pp. 84-94
    • Boelens, R.1    Rademaker, H.2    Pel, R.3    Wever, R.4
  • 14
    • 0021116608 scopus 로고
    • An EPR study of the photodissociation reactions of oxidized cytochrome c oxidase-nitric oxide complexes
    • Boelens R., Wever R., Van Gelder B.F., Rademaker H. An EPR study of the photodissociation reactions of oxidized cytochrome c oxidase-nitric oxide complexes. Biochim. Biophys. Acta. 724:1983;176-183.
    • (1983) Biochim. Biophys. Acta , vol.724 , pp. 176-183
    • Boelens, R.1    Wever, R.2    Van Gelder, B.F.3    Rademaker, H.4
  • 15
    • 0021772865 scopus 로고
    • The cytochrome c oxidase-azide-nitric oxide complex as a model for the oxygen binding site
    • Boelens R., Rademaker H., Wever R., Van Gelder B.F. The cytochrome c oxidase-azide-nitric oxide complex as a model for the oxygen binding site. Biochim. Biophys. Acta. 765:1984;196-209.
    • (1984) Biochim. Biophys. Acta , vol.765 , pp. 196-209
    • Boelens, R.1    Rademaker, H.2    Wever, R.3    Van Gelder, B.F.4
  • 18
    • 0017859629 scopus 로고
    • A spectroscopic study of nitric oxide-treated ceruloplasmin
    • Van Leeuwen F.X.R., van Gelder B.F. A spectroscopic study of nitric oxide-treated ceruloplasmin. Eur. J. Biochem. 87:1978;305-312.
    • (1978) Eur. J. Biochem. , vol.87 , pp. 305-312
    • Van Leeuwen, F.X.R.1    Van Gelder, B.F.2
  • 19
    • 0019758394 scopus 로고
    • Purification and properties of bovine ceruloplasmin
    • Calabrese L., Malatesta F., Barra D. Purification and properties of bovine ceruloplasmin. Biochem. J. 199:1981;667-673.
    • (1981) Biochem. J. , vol.199 , pp. 667-673
    • Calabrese, L.1    Malatesta, F.2    Barra, D.3
  • 20
    • 0025936158 scopus 로고
    • Interaction of nitric oxide with ceruloplasmin lacking an EPR detectable type 2 copper
    • Musci G., Di Marco S., Bonaccorsi di Patti M.C., Calabrese L. Interaction of nitric oxide with ceruloplasmin lacking an EPR detectable type 2 copper. Biochemistry. 30:1991;9866-9872.
    • (1991) Biochemistry , vol.30 , pp. 9866-9872
    • Musci, G.1    Di Marco, S.2    Bonaccorsi Di Patti, M.C.3    Calabrese, L.4
  • 22
    • 0016593451 scopus 로고
    • The reaction of nitric oxide with Rhus vernicifera laccase
    • Rotilio G., Morpurgo L., Graziani M.T., Brunori M. The reaction of nitric oxide with Rhus vernicifera laccase. FEBS Lett. 54:1975;163-166.
    • (1975) FEBS Lett. , vol.54 , pp. 163-166
    • Rotilio, G.1    Morpurgo, L.2    Graziani, M.T.3    Brunori, M.4
  • 26
    • 0009760043 scopus 로고    scopus 로고
    • Possible interaction of nitric oxide with the ferryl intermediate of cytochrome c oxidase
    • Torres J., Cooper C.E., Wilson M.T. Possible interaction of nitric oxide with the ferryl intermediate of cytochrome c oxidase. Biochem. Soc. Trans. 450S:1996;24.
    • (1996) Biochem. Soc. Trans. , vol.450 , pp. 24
    • Torres, J.1    Cooper, C.E.2    Wilson, M.T.3
  • 27
    • 0031559913 scopus 로고    scopus 로고
    • Nitric oxide ejects electrons from the binuclear centre of cytochrome c oxidase by reacting with oxidised copper: A general mechanism for the interaction of copper proteins with nitric oxide?
    • Cooper C.E., Torres J., Sharpe M., Wilson M.T. Nitric oxide ejects electrons from the binuclear centre of cytochrome c oxidase by reacting with oxidised copper: a general mechanism for the interaction of copper proteins with nitric oxide? FEBS Lett. 414:1997;281-284.
    • (1997) FEBS Lett. , vol.414 , pp. 281-284
    • Cooper, C.E.1    Torres, J.2    Sharpe, M.3    Wilson, M.T.4
  • 28
    • 0032502730 scopus 로고    scopus 로고
    • A common mechanism for the interaction of nitric oxide with the oxidized binuclear centre and oxygen intermediates of cytochrome c oxidase
    • Torres J., Cooper C.E., Wilson M.T. A common mechanism for the interaction of nitric oxide with the oxidized binuclear centre and oxygen intermediates of cytochrome c oxidase. J. Biol. Chem. 273:1998;8756-8766.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8756-8766
    • Torres, J.1    Cooper, C.E.2    Wilson, M.T.3
  • 30
    • 0344903526 scopus 로고
    • in: T.G. Spiro (Ed.), Wiley Interscience, New York, chapter 3.
    • B. Reinhammar, B.G. Malmstrom, in: T.G. Spiro (Ed.), Copper Proteins, Wiley Interscience, New York, 1981, chapter 3.
    • (1981) Copper Proteins
    • Reinhammar, B.1    Malmstrom, B.G.2
  • 33
    • 0014681476 scopus 로고
    • Studies of the heme components of cytochrome c oxidase by EPR spectroscopy
    • Van Gelder B.F., Beinert H. Studies of the heme components of cytochrome c oxidase by EPR spectroscopy. Biochim. Biophys. Acta. 189:1969;1-24.
    • (1969) Biochim. Biophys. Acta , vol.189 , pp. 1-24
    • Van Gelder, B.F.1    Beinert, H.2
  • 35
    • 0024287742 scopus 로고
    • Chicken ceruloplasmin. Evidence in support of a trinuclear cluster involving type 2 and 3 copper centers
    • Calabrese L., Carbonaro M., Musci G. Chicken ceruloplasmin. Evidence in support of a trinuclear cluster involving type 2 and 3 copper centers. J. Biol. Chem. 263:1988;6480-6483.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6480-6483
    • Calabrese, L.1    Carbonaro, M.2    Musci, G.3
  • 36
    • 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 L.-S., Spira-Solomon D.J., Penner-Hann J.E., Hodgson K.O., Solomon E.I. 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. 109:1987;6433-6442.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 6433-6442
    • Kau, L.-S.1    Spira-Solomon, D.J.2    Penner-Hann, J.E.3    Hodgson, K.O.4    Solomon, E.I.5
  • 37
    • 0022066911 scopus 로고
    • Low temperature magnetic circular dichroism studies of native laccase: Spectroscopic evidence for exogenous ligand bridging at a trinuclear copper active site
    • Allendorf M.D., Spira D.J., Solomon E.I. Low temperature magnetic circular dichroism studies of native laccase: spectroscopic evidence for exogenous ligand bridging at a trinuclear copper active site. Proc. Natl. Acad. Sci. USA. 82:1985;3063-3067.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3063-3067
    • Allendorf, M.D.1    Spira, D.J.2    Solomon, E.I.3
  • 39
    • 0017118855 scopus 로고
    • Kinetic studies of Rhus vernicifera laccase. Evidence for a multielectron transfer and an oxygen intermediate in the reoxidation reaction
    • Andreasson L.-E., Bränden R., Reinhammar B. Kinetic studies of Rhus vernicifera laccase. Evidence for a multielectron transfer and an oxygen intermediate in the reoxidation reaction. Biochim. Biophys. Acta. 438:1976;370-379.
    • (1976) Biochim. Biophys. Acta , vol.438 , pp. 370-379
    • Andreasson, L.-E.1    Bränden, R.2    Reinhammar, B.3
  • 40
    • 0027196880 scopus 로고
    • X-ray structures and mechanistic implications of 3 functional-derivatives of ascorbate oxidase from zucchini-reduced, peroxide and azide forms
    • Messerschmidt A., Luecke H., Huber R. X-ray structures and mechanistic implications of 3 functional-derivatives of ascorbate oxidase from zucchini-reduced, peroxide and azide forms. J. Mol. Biol. 230:1993;997-1014.
    • (1993) J. Mol. Biol. , vol.230 , pp. 997-1014
    • Messerschmidt, A.1    Luecke, H.2    Huber, R.3
  • 42
    • 0017152398 scopus 로고
    • Selective removal of type 2 copper from Rhus vernicifera laccase
    • Graziani M.T., Morpurgo L., Rotilio G., Mondovi B. Selective removal of type 2 copper from Rhus vernicifera laccase. FEBS Lett. 70:1976;87-90.
    • (1976) FEBS Lett. , vol.70 , pp. 87-90
    • Graziani, M.T.1    Morpurgo, L.2    Rotilio, G.3    Mondovi, B.4
  • 43
    • 0001138668 scopus 로고
    • Mixed-metal derivative of laccase containing mercury (II) in the type-1 binding-site
    • Morie-Bebel M.M., Morris M.C., Menzie J.L., McMillin D.R. Mixed-metal derivative of laccase containing mercury (II) in the type-1 binding-site. J. Am. Chem. Soc. 106:1984;3677-3678.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 3677-3678
    • Morie-Bebel, M.M.1    Morris, M.C.2    Menzie, J.L.3    McMillin, D.R.4
  • 44
    • 0025246697 scopus 로고
    • Reactivity of the laccase trinuclear copper active-site with dioxygen- an x-ray absorption-edge study
    • Cole J.L., Tan G.O., Yang E.K., Hodgson K.O., Solomon E.I. Reactivity of the laccase trinuclear copper active-site with dioxygen- an x-ray absorption-edge study. J. Am. Chem. Soc. 112:1990;2243-2249.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 2243-2249
    • Cole, J.L.1    Tan, G.O.2    Yang, E.K.3    Hodgson, K.O.4    Solomon, E.I.5
  • 47
    • 0342881368 scopus 로고
    • Spectroscopic characterization of the peroxide intermediate in the reduction of dioxygen catalyzed by the multicopper oxidases
    • Cole J.L., Ballou D.P., Solomon E.I. Spectroscopic characterization of the peroxide intermediate in the reduction of dioxygen catalyzed by the multicopper oxidases. J. Am. Chem. Soc. 113:1991;8544-8546.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 8544-8546
    • Cole, J.L.1    Ballou, D.P.2    Solomon, E.I.3
  • 48
    • 0030567363 scopus 로고    scopus 로고
    • Chemical and spectroscopic definition of the peroxide-level intermediate in the multicopper oxidases: Relevance to the catalytic mechanism of dioxygen reduction to water
    • Shin W., Sundaram V.M., Cole J.L., Zhang H.H., Hedman B., Hodgson K.O., Solomon E.I. Chemical and spectroscopic definition of the peroxide-level intermediate in the multicopper oxidases: relevance to the catalytic mechanism of dioxygen reduction to water. J. Am. Chem. Soc. 118:1996;3202-3215.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3202-3215
    • Shin, W.1    Sundaram, V.M.2    Cole, J.L.3    Zhang, H.H.4    Hedman, B.5    Hodgson, K.O.6    Solomon, E.I.7
  • 50
    • 0027401711 scopus 로고
    • Antioxidant protection against organic and inorganic oxygen radicals by normal human plasma: The important primary role for iron binding and iron-oxidizing proteins
    • Gutteridge J.M.C., Quinlan G.J. Antioxidant protection against organic and inorganic oxygen radicals by normal human plasma: the important primary role for iron binding and iron-oxidizing proteins. Biochim. Biophys. Acta. 1156:1992;144-150.
    • (1992) Biochim. Biophys. Acta , vol.1156 , pp. 144-150
    • Gutteridge, J.M.C.1    Quinlan, G.J.2
  • 51
    • 7744231498 scopus 로고    scopus 로고
    • Mechanisms whereby mononuclear copper proteins functionalize organic substrates
    • Klinman J.P. Mechanisms whereby mononuclear copper proteins functionalize organic substrates. Chem. Rev. 96:1996;2541-2561.
    • (1996) Chem. Rev. , vol.96 , pp. 2541-2561
    • Klinman, J.P.1
  • 52
    • 0023952257 scopus 로고
    • Dopamine β-hydroxylase of adrenal chromaffin granules: Structure and function
    • Stewart L.C., Klinman J.P. Dopamine β-hydroxylase of adrenal chromaffin granules: structure and function. Annu. Rev. Biochem. 57:1988;551-592.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 551-592
    • Stewart, L.C.1    Klinman, J.P.2
  • 53
    • 0025025585 scopus 로고
    • Characterization of a carbon-monoxide complex of reduced dopamine β-hydroxylase - evidence for inequivalence of the Cu(I) centers
    • Blackburn N.J., Pettingill T.M., Seagraves K.S., Shigeta R.T. Characterization of a carbon-monoxide complex of reduced dopamine β-hydroxylase - evidence for inequivalence of the Cu(I) centers. J. Biol. Chem. 265:1990;15383-15386.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15383-15386
    • Blackburn, N.J.1    Pettingill, T.M.2    Seagraves, K.S.3    Shigeta, R.T.4
  • 54
    • 0021109438 scopus 로고
    • Mechanism and modulation of dopamine β-monooxygenase by pH and fumarate as deduced from initial rate and primary deuterium isotope effect studies
    • Ahn N., Klinman J.P. Mechanism and modulation of dopamine β-monooxygenase by pH and fumarate as deduced from initial rate and primary deuterium isotope effect studies. Biochemistry. 22:1983;3096-3106.
    • (1983) Biochemistry , vol.22 , pp. 3096-3106
    • Ahn, N.1    Klinman, J.P.2
  • 55
    • 0029739477 scopus 로고    scopus 로고
    • Structural investigations of the coordination environment of the active site copper centres of recombinant bifunctional peptidylglycine α-amidating enzyme
    • Boswell J.S., Reedy B.J., Kulathila R., Merkler D.J., Blackburn N.J. Structural investigations of the coordination environment of the active site copper centres of recombinant bifunctional peptidylglycine α-amidating enzyme. Biochemistry. 35:1996;12241-12250.
    • (1996) Biochemistry , vol.35 , pp. 12241-12250
    • Boswell, J.S.1    Reedy, B.J.2    Kulathila, R.3    Merkler, D.J.4    Blackburn, N.J.5
  • 57
    • 0027159780 scopus 로고
    • Ligand interactions with galactose oxidase: Mechanistic insights
    • Whittaker M.M., Whittaker J.W. Ligand interactions with galactose oxidase: mechanistic insights. Biophys. J. 64:1993;762-772.
    • (1993) Biophys. J. , vol.64 , pp. 762-772
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 58
    • 0027965409 scopus 로고
    • Generation of the topa quinone cofactor in bacterial monoamino oxidase by cupric ion-independent autooxidation of a specific tyrosyl residue
    • Matsuzaki R., Fukui T., Sata H., Ozaki Y., Tanizawa K. Generation of the topa quinone cofactor in bacterial monoamino oxidase by cupric ion-independent autooxidation of a specific tyrosyl residue. FEBS Lett. 351:1994;360-364.
    • (1994) FEBS Lett. , vol.351 , pp. 360-364
    • Matsuzaki, R.1    Fukui, T.2    Sata, H.3    Ozaki, Y.4    Tanizawa, K.5
  • 59
    • 0028964417 scopus 로고
    • Copper/topa quinone-containing histamine oxidase from Arthrobacter globiformis. Molecular cloning and sequencing, overproduction of precursor enzyme and generation of topa quinone cofactor
    • Choi Y.H., Matsuzaki R., Fukui T., Shimizu E., Yorifuji T., Sata H., Ozaki Y., Tanizawa K. Copper/topa quinone-containing histamine oxidase from Arthrobacter globiformis. Molecular cloning and sequencing, overproduction of precursor enzyme and generation of topa quinone cofactor. J. Biol. Chem. 270:1995;4712-4720.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4712-4720
    • Choi, Y.H.1    Matsuzaki, R.2    Fukui, T.3    Shimizu, E.4    Yorifuji, T.5    Sata, H.6    Ozaki, Y.7    Tanizawa, K.8
  • 60
    • 0001202880 scopus 로고
    • Synthesis and structural and spectroscopic characterization of mononuclear copper nitrosyl complexes - models for nitric-oxide adducts of copper proteins and copper-exchanged zeolites
    • Ruggiero C.E., Carrier S.M., Antholine W.E., Whittaker J.W., Cramer C.J., Tolman W.B. Synthesis and structural and spectroscopic characterization of mononuclear copper nitrosyl complexes - models for nitric-oxide adducts of copper proteins and copper-exchanged zeolites. J. Am. Chem. Soc. 115:1993;11285-11298.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 11285-11298
    • Ruggiero, C.E.1    Carrier, S.M.2    Antholine, W.E.3    Whittaker, J.W.4    Cramer, C.J.5    Tolman, W.B.6


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