메뉴 건너뛰기




Volumn 9, Issue 2, 2005, Pages 152-163

Dioxygen activation by copper, heme and non-heme iron enzymes: Comparison of electronic structures and reactivities

Author keywords

[No Author keywords available]

Indexed keywords

COPPER DERIVATIVE; ENZYME; HEME DERIVATIVE; IRON DERIVATIVE;

EID: 16244423655     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2005.02.012     Document Type: Review
Times cited : (211)

References (57)
  • 2
    • 4644275807 scopus 로고    scopus 로고
    • Mechanism of oxidation reactions catalyzed by cytochrome P450 enzymes
    • B. Meunier, S.P. de Visser, and S. Shaik Mechanism of oxidation reactions catalyzed by cytochrome P450 enzymes Chem Rev 104 2004 3947 3980
    • (2004) Chem Rev , vol.104 , pp. 3947-3980
    • Meunier, B.1    De Visser, S.P.2    Shaik, S.3
  • 4
    • 1542378704 scopus 로고    scopus 로고
    • Dioxygen activation at mononuclear nonheme iron active sites: Enzymes, models, and intermediates
    • M. Costas, M.P. Mehn, M.P. Jensen, and L. Que Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates Chem Rev 104 2004 939 986
    • (2004) Chem Rev , vol.104 , pp. 939-986
    • Costas, M.1    Mehn, M.P.2    Jensen, M.P.3    Que, L.4
  • 6
    • 4644295937 scopus 로고    scopus 로고
    • Oxidant types in copper-dioxygen chemistry: The ligand coordination defines the Cu-n-O-2 structure and subsequent reactivity
    • L.Q. Hatcher, and K.D. Karlin Oxidant types in copper-dioxygen chemistry: the ligand coordination defines the Cu-n-O-2 structure and subsequent reactivity J Biol Inorg Chem 9 2004 669 683
    • (2004) J Biol Inorg Chem , vol.9 , pp. 669-683
    • Hatcher, L.Q.1    Karlin, K.D.2
  • 7
    • 11544259897 scopus 로고    scopus 로고
    • Cleavage of nucleic acids by bleomycin
    • R.M. Burger Cleavage of nucleic acids by bleomycin Chem Rev 98 1998 1153 1169
    • (1998) Chem Rev , vol.98 , pp. 1153-1169
    • Burger, R.M.1
  • 8
    • 0033980083 scopus 로고    scopus 로고
    • Bleomycin: New perspectives on the mechanism of action
    • S.M. Hecht Bleomycin: new perspectives on the mechanism of action J Nat Prod 63 2000 158 168
    • (2000) J Nat Prod , vol.63 , pp. 158-168
    • Hecht, S.M.1
  • 9
    • 1842426944 scopus 로고    scopus 로고
    • Bleomycins: New methods will allow reinvestigation of old issues
    • J.Y. Chen, and J.A. Stubbe Bleomycins: new methods will allow reinvestigation of old issues Curr Opin Chem Biol 8 2004 175 181
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 175-181
    • Chen, J.Y.1    Stubbe, J.A.2
  • 10
    • 0020645721 scopus 로고
    • Mössbauer study of iron bleomycin and its activation intermediates
    • R.M. Burger, T.A. Kent, S.B. Horwitz, E. Münck, and J. Peisach Mössbauer study of iron bleomycin and its activation intermediates J Biol Chem 258 1983 1559 1564
    • (1983) J Biol Chem , vol.258 , pp. 1559-1564
    • Burger, R.M.1    Kent, T.A.2    Horwitz, S.B.3    Münck, E.4    Peisach, J.5
  • 11
    • 0027991713 scopus 로고
    • Electrospray mass spectrometry of iron bleomycin: Demonstration that activated bleomycin is a ferric peroxide complex
    • J.W. Sam, X.-J. Tang, and J. Peisach Electrospray mass spectrometry of iron bleomycin: demonstration that activated bleomycin is a ferric peroxide complex J Am Chem Soc 116 1994 3250 5256
    • (1994) J Am Chem Soc , vol.116 , pp. 3250-5256
    • Sam, J.W.1    Tang, X.-J.2    Peisach, J.3
  • 12
    • 0034731019 scopus 로고    scopus 로고
    • Electronic structure of activated bleomycin: Oxygen intermediates in heme versus non-heme iron
    • F. Neese, J.M. Zaleski, K. Loeb Zaleski, and E.I. Solomon Electronic structure of activated bleomycin: oxygen intermediates in heme versus non-heme iron J Am Chem Soc 122 2000 11703 11724
    • (2000) J Am Chem Soc , vol.122 , pp. 11703-11724
    • Neese, F.1    Zaleski, J.M.2    Loeb Zaleski, K.3    Solomon, E.I.4
  • 13
    • 0001080723 scopus 로고    scopus 로고
    • Nature of activated bleomycin
    • R.M. Burger Nature of activated bleomycin Struct Bonding 97 2000 287 303
    • (2000) Struct Bonding , vol.97 , pp. 287-303
    • Burger, R.M.1
  • 14
    • 0000767074 scopus 로고    scopus 로고
    • Role of the heme active site and protein environment in structure, spectra, and function of the cytochrome p450s
    • G.H. Loew, and D.L. Harris Role of the heme active site and protein environment in structure, spectra, and function of the cytochrome p450s Chem Rev 100 2000 407 419
    • (2000) Chem Rev , vol.100 , pp. 407-419
    • Loew, G.H.1    Harris, D.L.2
  • 15
    • 0035606245 scopus 로고    scopus 로고
    • High-valent intermediates of heme proteins and model compounds
    • D.L. Harris High-valent intermediates of heme proteins and model compounds Curr Opin Chem Biol 5 2001 724 735
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 724-735
    • Harris, D.L.1
  • 18
    • 4644268354 scopus 로고    scopus 로고
    • One oxidant, many pathways: A theoretical perspective of monooxygenation mechanisms by cytochrome P450 enzymes
    • • ]) focuses on the biochemical, biomimetic and computational aspects of the ongoing discussion on whether the iron(IV)-oxo porphyrin cation-radical, CpI, is the sole oxidizing species in heme systems such as cytochrome p450, or whether a hydroperoxoferric intermediate functions as a second oxidant.
    • (2004) J Biol Inorg Chem , vol.9 , pp. 661-668
    • Shaik, S.1    De Visser, S.P.2    Kumar, D.3
  • 19
    • 0033623690 scopus 로고    scopus 로고
    • Hypersensitive radical probes and the mechanisms of cytochrome P450-catalyzed hydroxylation reactions
    • M. Newcomb, and P.H. Toy Hypersensitive radical probes and the mechanisms of cytochrome P450-catalyzed hydroxylation reactions Acc Chem Res 33 2000 449 455
    • (2000) Acc Chem Res , vol.33 , pp. 449-455
    • Newcomb, M.1    Toy, P.H.2
  • 20
    • 0037228374 scopus 로고    scopus 로고
    • Multiple mechanisms and multiple oxidants in P450-catalyzed hydroxylations
    • M. Newcomb, P.F. Hollenberg, and M.J. Coon Multiple mechanisms and multiple oxidants in P450-catalyzed hydroxylations Arch Biochem Biophys 409 2003 72 79
    • (2003) Arch Biochem Biophys , vol.409 , pp. 72-79
    • Newcomb, M.1    Hollenberg, P.F.2    Coon, M.J.3
  • 21
    • 0037389990 scopus 로고    scopus 로고
    • Non-heme iron enzymes: Contrasts to heme catalysis
    • E.I. Solomon, A. Decker, and N. Lehnert Non-heme iron enzymes: contrasts to heme catalysis Proc Natl Acad Sci USA 100 2003 3589 3594 This perspective compares the homolytic and heterolytic OO bond cleavage in heme and non-heme ferric-hydroperoxo species and the electronic structures of the high valent Fe-oxo products. It shows that while for heme systems heterolytic cleavage and iron(IV)-oxo porphyrin radical is accessible, this process is energetically too unfavorable for non-heme ligand sets, which instead can undergo homolytic cleavage and formation of a Fe(IV)O species.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3589-3594
    • Solomon, E.I.1    Decker, A.2    Lehnert, N.3
  • 22
    • 0037130661 scopus 로고    scopus 로고
    • A density functional study of O-O bond cleavage for a biomimetic non-heme iron complex demonstrating an Fev-intermediate
    • A. Bassan, M.R.A. Blomberg, P.E.M. Siegbahn, and L. Que A density functional study of O-O bond cleavage for a biomimetic non-heme iron complex demonstrating an Fev-intermediate J Am Chem Soc 124 2002 11056 11063
    • (2002) J Am Chem Soc , vol.124 , pp. 11056-11063
    • Bassan, A.1    Blomberg, M.R.A.2    Siegbahn, P.E.M.3    Que, L.4
  • 23
    • 0029670557 scopus 로고    scopus 로고
    • 2 green: Its detailed structural characterization by NMR and molecular modeling and its sequence-specific interaction with DNA oligonucleotides
    • 2 green: its detailed structural characterization by NMR and molecular modeling and its sequence-specific interaction with DNA oligonucleotides J Am Chem Soc 118 1996 1268 1280
    • (1996) J Am Chem Soc , vol.118 , pp. 1268-1280
    • Wu, W.1    Vanderwall, D.E.2    Lui, S.M.3    Tang, X.-J.4    Turner, C.J.5    Kozarich, J.W.6    Stubbe, J.7
  • 24
    • 4644302003 scopus 로고    scopus 로고
    • The oxo/peroxo debate: A nonheme iron perspective
    • L. Que The oxo/peroxo debate: a nonheme iron perspective J Biol Inorg Chem 9 2004 684 690
    • (2004) J Biol Inorg Chem , vol.9 , pp. 684-690
    • Que, L.1
  • 26
    • 2342472569 scopus 로고    scopus 로고
    • Spectroscopic and quantum chemical characterization of the electronic structure and bonding in a non-heme Fe-IVO complex
    • IVO (S = 1) complex. Spectroscopic methods and experimentally calibrated density functional calculations were used to elucidate very strong σ- and π FeO bonding and correlate the S = 1 and S = 2 spin states.
    • (2004) J Am Chem Soc , vol.126 , pp. 5378-5379
    • Decker, A.1    Rohde, J.-U.2    Que Jr., L.3    Solomon, E.I.4
  • 27
    • 0034809080 scopus 로고    scopus 로고
    • Spectroscopic properties and electronic structure of low-spin Fe(III)-alkylperoxo complexes: Homolytic cleavage of the OO bond
    • N. Lehnert, R.Y.N. Ho, L. Que Jr., and E.I. Solomon Spectroscopic properties and electronic structure of low-spin Fe(III)-alkylperoxo complexes: homolytic cleavage of the OO bond J Am Chem Soc 123 2001 8271 8290
    • (2001) J Am Chem Soc , vol.123 , pp. 8271-8290
    • Lehnert, N.1    Ho, R.Y.N.2    Que Jr., L.3    Solomon, E.I.4
  • 28
    • 0035956535 scopus 로고    scopus 로고
    • Electronic structure of high-spin iron(III)-alkylperoxo complexes and its relation to low-spin analogues: Reaction coordinate of OO bond homolysis
    • N. Lehnert, Ho RYN, L. Que Jr., and E.I. Solomon Electronic structure of high-spin iron(III)-alkylperoxo complexes and its relation to low-spin analogues: reaction coordinate of OO bond homolysis J Am Chem Soc 123 2001 12802 12816
    • (2001) J Am Chem Soc , vol.123 , pp. 12802-12816
    • Lehnert, N.1    Ho, R.Y.N.2    Que Jr., L.3    Solomon, E.I.4
  • 29
    • 0037063569 scopus 로고    scopus 로고
    • Electronic structure and reactivity of low-spin Fe(III)-hydroperoxo complexes: Comparison to activated bleomycin
    • N. Lehnert, R.Y.N. Ho, F. Neese, L. Que Jr., and E.I. Solomon Electronic structure and reactivity of low-spin Fe(III)-hydroperoxo complexes: comparison to activated bleomycin J Am Chem Soc 124 2002 10810 10822
    • (2002) J Am Chem Soc , vol.124 , pp. 10810-10822
    • Lehnert, N.1    Ho, R.Y.N.2    Neese, F.3    Que Jr., L.4    Solomon, E.I.5
  • 30
    • 7244258076 scopus 로고    scopus 로고
    • The reduction pathway of end-on coordinated dinitrogen. I. Vibrational spectra of Mo/W-N-2, -NNH, and -NNH2 complexes and quantum chemistry assisted normal coordinate analysis
    • N. Lehnert, and F. Tuczek The reduction pathway of end-on coordinated dinitrogen. I. Vibrational spectra of Mo/W-N-2, -NNH, and -NNH2 complexes and quantum chemistry assisted normal coordinate analysis Inorg Chem 38 1999 1659 1670
    • (1999) Inorg Chem , vol.38 , pp. 1659-1670
    • Lehnert, N.1    Tuczek, F.2
  • 31
    • 33845283437 scopus 로고
    • Vibrational electronic and resonance Raman spectral studies of a copper-II peroxide model complex of oxyhemocyanin
    • J.E. Pate, R.W. Cruse, K.D. Karlin, and E.I. Solomon Vibrational electronic and resonance Raman spectral studies of a copper-II peroxide model complex of oxyhemocyanin J Am Chem Soc 109 1987 2624 2630
    • (1987) J Am Chem Soc , vol.109 , pp. 2624-2630
    • Pate, J.E.1    Cruse, R.W.2    Karlin, K.D.3    Solomon, E.I.4
  • 32
    • 0001218731 scopus 로고
    • A mechanistic probe for oxygen activation by metal-complexes and hydroperoxides and its application to alkane functionalization by [Fe(III)Cl(2)tris(2-pyridinylmethyl)amine](+)BF4
    • I.W.C.E. Arends, K.U. Ingold, and D.D.M. Wayner A mechanistic probe for oxygen activation by metal-complexes and hydroperoxides and its application to alkane functionalization by [Fe(III)Cl(2)tris(2-pyridinylmethyl)amine](+)BF4- J Am Chem Soc 117 1995 4710 4711
    • (1995) J Am Chem Soc , vol.117 , pp. 4710-4711
    • Arends, I.W.C.E.1    Ingold, K.U.2    Wayner, D.D.M.3
  • 33
    • 0000845585 scopus 로고    scopus 로고
    • Oxygen activation by metal complexes and alkyl hydroperoxides. Applications of mechanistic probes to explore the role of alkoxyl radicals in alkane functionalization
    • P.A. MacFaul, I.W.C.E. Arends, K.U. Ingold, and D.D.M. Wayner Oxygen activation by metal complexes and alkyl hydroperoxides. Applications of mechanistic probes to explore the role of alkoxyl radicals in alkane functionalization J Chem Soc, Perkin Trans 1 1997 135 145
    • (1997) J Chem Soc, Perkin Trans 1 , pp. 135-145
    • MacFaul, P.A.1    Arends, I.W.C.E.2    Ingold, K.U.3    Wayner, D.D.M.4
  • 34
    • 0030728024 scopus 로고    scopus 로고
    • A putative monooxygenase mimic which functions via well-disguised free radical chemistry
    • P.A. MacFaul, K.U. Ingold, D.D.M. Wayner, and L. Que A putative monooxygenase mimic which functions via well-disguised free radical chemistry J Am Chem Soc 119 1997 10594 10598
    • (1997) J Am Chem Soc , vol.119 , pp. 10594-10598
    • MacFaul, P.A.1    Ingold, K.U.2    Wayner, D.D.M.3    Que, L.4
  • 35
    • 0037181365 scopus 로고    scopus 로고
    • Olefin cis-dihydroxylation versus epoxidation by non-heme iron catalysts: Two faces of an FeIII-OOH coin
    • K. Chen, M. Costas, J.H. Kim, A.K. Tipton, and L. Que Olefin cis-dihydroxylation versus epoxidation by non-heme iron catalysts: two faces of an FeIII-OOH coin J Am Chem Soc 124 2002 3026 3035
    • (2002) J Am Chem Soc , vol.124 , pp. 3026-3035
    • Chen, K.1    Costas, M.2    Kim, J.H.3    Tipton, A.K.4    Que, L.5
  • 36
    • 0036026571 scopus 로고    scopus 로고
    • Spin state tuning of non-heme iron-catalyzed hydrocarbon oxidations: Participation of Fe-III-OOH and Fe-VO intermediates
    • K. Chen, M. Costas, and L. Que Spin state tuning of non-heme iron-catalyzed hydrocarbon oxidations: participation of Fe-III-OOH and Fe-VO intermediates J Chem Soc Dalton Trans 2002 672 679
    • (2002) J Chem Soc Dalton Trans , pp. 672-679
    • Chen, K.1    Costas, M.2    Que, L.3
  • 37
    • 0038747011 scopus 로고    scopus 로고
    • The first direct characterization of a high-valent iron intermediate in the reaction of an alpha-ketoglutarate-dependent dioxygenase: A high-spin Fe(IV) complex in taurine/alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli
    • J.C. Price, E.W. Barr, B. Tirupati, J.M. Bollinger, and C. Krebs The first direct characterization of a high-valent iron intermediate in the reaction of an alpha-ketoglutarate-dependent dioxygenase: a high-spin Fe(IV) complex in taurine/alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli Biochemistry 42 2003 7497 7508
    • (2003) Biochemistry , vol.42 , pp. 7497-7508
    • Price, J.C.1    Barr, E.W.2    Tirupati, B.3    Bollinger, J.M.4    Krebs, C.5
  • 38
    • 3042770458 scopus 로고    scopus 로고
    • EXAFS spectroscopic evidence for an Fe = O unit in the Fe(IV) intermediate observed during oxygen activation by taurine:alpha-ketoglutarate dioxygenase
    • P.J. Riggs-Gelasco, J.C. Price, R.B. Guyer, J.H. Brehm, E.W. Barr, J.M. Bollinger, and C. Krebs EXAFS spectroscopic evidence for an Fe = O unit in the Fe(IV) intermediate observed during oxygen activation by taurine:alpha- ketoglutarate dioxygenase J Am Chem Soc 126 2004 8108 8109
    • (2004) J Am Chem Soc , vol.126 , pp. 8108-8109
    • Riggs-Gelasco, P.J.1    Price, J.C.2    Guyer, R.B.3    Brehm, J.H.4    Barr, E.W.5    Bollinger, J.M.6    Krebs, C.7
  • 39
    • 0942298044 scopus 로고    scopus 로고
    • Direct detection of oxygen intermediates in the non-heme Fe enzyme taurine/alpha-ketoglutarate dioxygenase
    • D.A. Proshlyakov, T.F. Henshaw, G.R. Monterosso, M.J. Ryle, and R.P. Hausinger Direct detection of oxygen intermediates in the non-heme Fe enzyme taurine/alpha-ketoglutarate dioxygenase J Am Chem Soc 126 2004 1022 1023
    • (2004) J Am Chem Soc , vol.126 , pp. 1022-1023
    • Proshlyakov, D.A.1    Henshaw, T.F.2    Monterosso, G.R.3    Ryle, M.J.4    Hausinger, R.P.5
  • 40
    • 7744231498 scopus 로고    scopus 로고
    • Mechanisms whereby mononuclear copper proteins functionalize organic substrates
    • J.P. Klinman 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
  • 41
    • 0027982856 scopus 로고
    • Oxygen-18 kinetic isotope effects in the dopamine beta-monooxygenase reaction: Evidence for a new chemical mechanism in non-heme metallomonooxygenases
    • G.C. Tian, J.A. Berry, and J.P. Klinman Oxygen-18 kinetic isotope effects in the dopamine beta-monooxygenase reaction: evidence for a new chemical mechanism in non-heme metallomonooxygenases Biochemistry 33 1994 226 234
    • (1994) Biochemistry , vol.33 , pp. 226-234
    • Tian, G.C.1    Berry, J.A.2    Klinman, J.P.3
  • 42
    • 0034684243 scopus 로고    scopus 로고
    • Spectroscopic and theoretical studies of mononuclear copper(II) alkyl- and hydroperoxo complexes: Electronic structure contributions to reactivity
    • P. Chen, K. Fujisawa, and E.I. Solomon Spectroscopic and theoretical studies of mononuclear copper(II) alkyl- and hydroperoxo complexes: electronic structure contributions to reactivity J Am Chem Soc 122 2000 10177
    • (2000) J Am Chem Soc , vol.122 , pp. 10177
    • Chen, P.1    Fujisawa, K.2    Solomon, E.I.3
  • 43
    • 1942504122 scopus 로고    scopus 로고
    • Oxygen activation by the noncoupled binuclear copper site in peptidylglycine alpha-hydroxylating monooxygenase. Reaction mechanism and role of the noncoupled nature of the active site
    • P. Chen, and E.I. Solomon Oxygen activation by the noncoupled binuclear copper site in peptidylglycine alpha-hydroxylating monooxygenase. Reaction mechanism and role of the noncoupled nature of the active site J Am Chem Soc 126 2004 4991 5000
    • (2004) J Am Chem Soc , vol.126 , pp. 4991-5000
    • Chen, P.1    Solomon, E.I.2
  • 44
    • 2442444490 scopus 로고    scopus 로고
    • Oxygen activation by the noncoupled binuclear copper site in peptidylglycine alpha-hydroxylating monooxygenase. Spectroscopic definition of the resting sites and the putative CuIIM-OOH intermediate
    • P. Chen, J. Bell, B.A. Eipper, and E.I. Solomon Oxygen activation by the noncoupled binuclear copper site in peptidylglycine alpha-hydroxylating monooxygenase. Spectroscopic definition of the resting sites and the putative CuIIM-OOH intermediate Biochemistry 43 2004 5735 5747
    • (2004) Biochemistry , vol.43 , pp. 5735-5747
    • Chen, P.1    Bell, J.2    Eipper, B.A.3    Solomon, E.I.4
  • 46
    • 0001326190 scopus 로고
    • Electronic structure of peroxide-bridged copper dimers of relevance to oxyhemocyanin
    • P.K. Ross, and E.I. Solomon Electronic structure of peroxide-bridged copper dimers of relevance to oxyhemocyanin J Am Chem Soc 112 1990 5871 5872
    • (1990) J Am Chem Soc , vol.112 , pp. 5871-5872
    • Ross, P.K.1    Solomon, E.I.2
  • 47
    • 84961981271 scopus 로고    scopus 로고
    • Dioxygen binding to deoxyhemocyanin: Electronic structure and mechanism of the spin-forbidden two-electron reduction of O-2
    • M. Metz, and E.I. Solomon Dioxygen binding to deoxyhemocyanin: electronic structure and mechanism of the spin-forbidden two-electron reduction of O-2 J Am Chem Soc 123 2001 4938 4950
    • (2001) J Am Chem Soc , vol.123 , pp. 4938-4950
    • Metz, M.1    Solomon, E.I.2
  • 48
    • 1542304579 scopus 로고    scopus 로고
    • Structure and spectroscopy of copper-dioxygen complexes
    • L.M. Mirica, X. Ottenwaelder, and TD.P. Stack Structure and spectroscopy of copper-dioxygen complexes Chem Rev 104 2004 1013 1045
    • (2004) Chem Rev , vol.104 , pp. 1013-1045
    • Mirica, L.M.1    Ottenwaelder, X.2    Stack, T.P.3
  • 49
    • 1542288709 scopus 로고    scopus 로고
    • Reactivity of dioxygen-copper systems
    • E.A. Lewis, and W.B. Tolman Reactivity of dioxygen-copper systems Chem Rev 104 2004 1047 1076
    • (2004) Chem Rev , vol.104 , pp. 1047-1076
    • Lewis, E.A.1    Tolman, W.B.2
  • 50
    • 0033544352 scopus 로고    scopus 로고
    • Spectroscopic and electronic structural studies of the Cu(III)(2) bis-mu-oxo core and its relation to the side-on peroxo-bridged dimer
    • M.J. Henson, P. Mukherjee, D.E. Root, Stack TDP, and E.I. Solomon Spectroscopic and electronic structural studies of the Cu(III)(2) bis-mu-oxo core and its relation to the side-on peroxo-bridged dimer J Am Chem Soc 121 1999 10332 10345
    • (1999) J Am Chem Soc , vol.121 , pp. 10332-10345
    • Henson, M.J.1    Mukherjee, P.2    Root, D.E.3    Stack, T.D.P.4    Solomon, E.I.5
  • 51
    • 0346118953 scopus 로고    scopus 로고
    • Evidence that dioxygen and substrate activation are tightly coupled in dopamine beta-monooxygenase. Implications for the reactive oxygen species
    • J.P. Evans, K. Ahn, and J.P. Klinman Evidence that dioxygen and substrate activation are tightly coupled in dopamine beta-monooxygenase. Implications for the reactive oxygen species J Biol Chem 278 2003 49691 49698 The tight coupling between dioxygen activation and CH bond cleavage observed for DβH is explained by proposing a diamagnetic copper-superoxo intermediate that carries out CH bond cleavage.
    • (2003) J Biol Chem , vol.278 , pp. 49691-49698
    • Evans, J.P.1    Ahn, K.2    Klinman, J.P.3
  • 52
    • 0030699146 scopus 로고    scopus 로고
    • Amidation of bioactive peptides: The structure of peptidylglycine alpha -hydroxylating monooxygenase
    • S.T. Prigge, A.S. Kolhekar, B.A. Eipper, R.E. Mains, and L.M. Amzel Amidation of bioactive peptides: the structure of peptidylglycine alpha -hydroxylating monooxygenase Science 278 1997 1300 1305
    • (1997) Science , vol.278 , pp. 1300-1305
    • Prigge, S.T.1    Kolhekar, A.S.2    Eipper, B.A.3    Mains, R.E.4    Amzel, L.M.5
  • 53
    • 0032861557 scopus 로고    scopus 로고
    • Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase
    • S.T. Prigge, A.S. Kolhekar, B.A. Eipper, R.E. Mains, and L.M. Amzel Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase Nat Struct Biol 6 1999 976 983
    • (1999) Nat Struct Biol , vol.6 , pp. 976-983
    • Prigge, S.T.1    Kolhekar, A.S.2    Eipper, B.A.3    Mains, R.E.4    Amzel, L.M.5
  • 55
    • 2442545587 scopus 로고    scopus 로고
    • Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex
    • + unit is the first example of a monocopper-dioxygen intermediate to be structurally defined in a protein.
    • (2004) Science , vol.304 , pp. 864-867
    • Prigge, S.T.1    Eipper, B.A.2    Mains, R.E.3    Amzel, L.M.4
  • 56
    • 4544332259 scopus 로고    scopus 로고
    • O-2 activation by binuclear Cu sites: Noncoupled versus exchange coupled reaction mechanisms
    • P. Chen, and E.I. Solomon O-2 activation by binuclear Cu sites: noncoupled versus exchange coupled reaction mechanisms Proc Natl Acad Sci USA 101 2004 13105 13110 This perspective correlates the different mechanisms in dioxygen activation of coupled and non-coupled binuclear copper enzymes and develops the concept that the extent of magnetic exchange coupling between Cu centers can tune the formation of different oxygen intermediates (peroxo versus superoxo) and thus control the reactivity (electrophilic attack versus H-atom abstraction).
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13105-13110
    • Chen, P.1    Solomon, E.I.2
  • 57
    • 16244405752 scopus 로고    scopus 로고
    • Comparison of FeIV=O heme and non-heme species: Electronic structures, bonding and reactivities
    • in press.
    • IV=O (S = 1) heme and non-heme species reveals an extremely similar electronic structure and FeO bonding, due to a decoupling of the dominating iron-oxo unit from the porphyrin π-system in the heme complex.
    • (2005) Angew Chem
    • Decker, A.1    Solomon, E.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.