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Volumn 344, Issue 3, 2004, Pages 599-607

Using xenon as a probe for dioxygen-binding sites in copper amine oxidases

Author keywords

amine oxidase; copper enzyme; dioxygen binding; xenon chamber; xenon protein complex

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING); COPPER DERIVATIVE; OXYGEN;

EID: 7944226404     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.09.075     Document Type: Article
Times cited : (55)

References (39)
  • 1
    • 0034792192 scopus 로고    scopus 로고
    • Trihydroxyphenylalanine quinine (TPQ) from copper amine oxidases and lysyl tyrosylquinone (LTQ) from lysyl oxidase
    • J.E. Dove, and J.P. Klinman Trihydroxyphenylalanine quinine (TPQ) from copper amine oxidases and lysyl tyrosylquinone (LTQ) from lysyl oxidase Advan. Protein Chem. 58 2001 141 174
    • (2001) Advan. Protein Chem. , vol.58 , pp. 141-174
    • Dove, J.E.1    Klinman, J.P.2
  • 3
    • 0035951098 scopus 로고    scopus 로고
    • Spectroscopic observation of intermediates formed durimg the oxidative half-reaction of copper/topa quinine-containing phenylethylamine oxidase
    • S. Hirota, T. Iwamoto, S. Kishishita, T. Okajima, O. Yamauchi, and K. Tanizawa Spectroscopic observation of intermediates formed durimg the oxidative half-reaction of copper/topa quinine-containing phenylethylamine oxidase Biochemistry 40 2001 15789 15796
    • (2001) Biochemistry , vol.40 , pp. 15789-15796
    • Hirota, S.1    Iwamoto, T.2    Kishishita, S.3    Okajima, T.4    Yamauchi, O.5    Tanizawa, K.6
  • 4
    • 0035182726 scopus 로고    scopus 로고
    • The reductive and oxidative half-reaction and the role of copper ions in plant and mammalian copper-amine oxidases
    • A. Padiglia, R. Medda, A. Bellelli, E. Agostinelli, L. Morpurgo, and B. Mondovi The reductive and oxidative half-reaction and the role of copper ions in plant and mammalian copper-amine oxidases Eur. J. Inorg. Chem. 1 2001 35 42
    • (2001) Eur. J. Inorg. Chem. , vol.1 , pp. 35-42
    • Padiglia, A.1    Medda, R.2    Bellelli, A.3    Agostinelli, E.4    Morpurgo, L.5    Mondovi, B.6
  • 5
    • 0032497371 scopus 로고    scopus 로고
    • Probing the mechanism of proton coupled electron transfer to dioxygen: The oxidative half-reaction of bovine serum amine oxidase
    • Q. Su, and J.P. Klinman Probing the mechanism of proton coupled electron transfer to dioxygen: the oxidative half-reaction of bovine serum amine oxidase Biochemistry 37 1998 12513 12525
    • (1998) Biochemistry , vol.37 , pp. 12513-12525
    • Su, Q.1    Klinman, J.P.2
  • 6
    • 0034603707 scopus 로고    scopus 로고
    • Kinetic analysis of oxygen utilization during cofactor biogenesis in a copper-containing amine oxidase from yeast
    • B. Schwartz, J.E. Dove, and J.P. Klinman Kinetic analysis of oxygen utilization during cofactor biogenesis in a copper-containing amine oxidase from yeast Biochemistry 39 2000 3699 3707
    • (2000) Biochemistry , vol.39 , pp. 3699-3707
    • Schwartz, B.1    Dove, J.E.2    Klinman, J.P.3
  • 7
    • 0034684215 scopus 로고    scopus 로고
    • + during dioxygen activation in a copper amine oxidase
    • + during dioxygen activation in a copper amine oxidase J. Am. Chem. Soc. 122 2000 9897 9904
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 9897-9904
    • Mills, S.A.1    Klinman, J.P.2
  • 8
    • 0037137223 scopus 로고    scopus 로고
    • Binding of dioxygen to non-metal sites in proteins: Exploration of the importance of binding site size versus hydrophobicity in the copper amine oxidase from Hansenula polymorpha
    • Y. Goto, and J.P. Klinman Binding of dioxygen to non-metal sites in proteins: exploration of the importance of binding site size versus hydrophobicity in the copper amine oxidase from Hansenula polymorpha Biochemistry 41 2002 13637 13643
    • (2002) Biochemistry , vol.41 , pp. 13637-13643
    • Goto, Y.1    Klinman, J.P.2
  • 10
    • 0034916716 scopus 로고    scopus 로고
    • Visualization of dioxygen bound to copper during enzyme catalysis
    • B.O. Elmore, and D.M. Dooley Visualization of dioxygen bound to copper during enzyme catalysis Chemtracts: Inorg. Chem. 14 2001 243 251
    • (2001) Chemtracts: Inorg. Chem. , vol.14 , pp. 243-251
    • Elmore, B.O.1    Dooley, D.M.2
  • 11
    • 0027250458 scopus 로고
    • Intramolecular electron transfer rate between active-site copper and topa quinone in pea seedling amine oxidase
    • P.N. Turowski, M.A. McGuirl, and D.M. Dooley Intramolecular electron transfer rate between active-site copper and topa quinone in pea seedling amine oxidase J. Biol. Chem. 268 1993 17680 17682
    • (1993) J. Biol. Chem. , vol.268 , pp. 17680-17682
    • Turowski, P.N.1    McGuirl, M.A.2    Dooley, D.M.3
  • 12
    • 84863393081 scopus 로고    scopus 로고
    • Intramolecular electron transfer in the oxidation of amines by methylamine oxidase from Arthrobacter P1
    • D.M. Dooley, and D.E. Brown Intramolecular electron transfer in the oxidation of amines by methylamine oxidase from Arthrobacter P1 J. Biol. Inorg. Chem. 1 1996 205 209
    • (1996) J. Biol. Inorg. Chem. , vol.1 , pp. 205-209
    • Dooley, D.M.1    Brown, D.E.2
  • 13
    • 1642271052 scopus 로고    scopus 로고
    • Theoretical study of the mechanism for the oxidative half-reaction of copper amine oxidase (CAO)
    • R. Prabhakar, and P.E.M. Siegbahn Theoretical study of the mechanism for the oxidative half-reaction of copper amine oxidase (CAO) J. Phys. Chem. B 107 2003 3944 3953
    • (2003) J. Phys. Chem. B , vol.107 , pp. 3944-3953
    • Prabhakar, R.1    Siegbahn, P.E.M.2
  • 14
    • 0037636501 scopus 로고    scopus 로고
    • A theoretical study of the dioxygen activation by glucose oxidase and copper amine oxidase
    • R. Prabhakar, P.E.M. Siegbahn, and B.F. Minaev A theoretical study of the dioxygen activation by glucose oxidase and copper amine oxidase Biochim. Biophys. Acta 1647 2003 173 178
    • (2003) Biochim. Biophys. Acta , vol.1647 , pp. 173-178
    • Prabhakar, R.1    Siegbahn, P.E.M.2    Minaev, B.F.3
  • 15
    • 0020180559 scopus 로고
    • Effects of media and electrode materials on the electrochemical reduction of dioxygen
    • D.T. Sawyer, G. Chiericato, C.T. Angelis, E.J. Nanni, and T. Tsuchiya Effects of media and electrode materials on the electrochemical reduction of dioxygen Anal. Chem. 54 1982 1720 1724
    • (1982) Anal. Chem. , vol.54 , pp. 1720-1724
    • Sawyer, D.T.1    Chiericato, G.2    Angelis, C.T.3    Nanni, E.J.4    Tsuchiya, T.5
  • 16
    • 0013842370 scopus 로고
    • Binding of xenon to sperm whale myoglobin
    • B.P. Schoenborn, H.C. Watson, and J.C. Kendrew Binding of xenon to sperm whale myoglobin Nature 207 1965 28 30
    • (1965) Nature , vol.207 , pp. 28-30
    • Schoenborn, B.P.1    Watson, H.C.2    Kendrew, J.C.3
  • 17
    • 0013851845 scopus 로고
    • Binding of xenon to horse haemoglobin
    • B.P. Schoenborn Binding of xenon to horse haemoglobin Nature 208 1965 760 762
    • (1965) Nature , vol.208 , pp. 760-762
    • Schoenborn, B.P.1
  • 18
    • 0021766921 scopus 로고
    • Cavities in proteins: Structure of a metmyoglobin-xenon complex solved to 1.9 Å
    • R.F. Tilton, I.D. Kuntz, and G.A. Petsko Cavities in proteins: structure of a metmyoglobin-xenon complex solved to 1.9 Å Biochemistry 23 1984 2849 2857
    • (1984) Biochemistry , vol.23 , pp. 2849-2857
    • Tilton, R.F.1    Kuntz, I.D.2    Petsko, G.A.3
  • 20
    • 0029644248 scopus 로고
    • The catalytic site of serine proteinases as a specific binding cavity for xenon
    • M. Schiltz, R. Fourme, I. Broutin, and T. Prangé The catalytic site of serine proteinases as a specific binding cavity for xenon Structure 3 1995 309 316
    • (1995) Structure , vol.3 , pp. 309-316
    • Schiltz, M.1    Fourme, R.2    Broutin, I.3    Prangé, T.4
  • 21
    • 0031180380 scopus 로고    scopus 로고
    • Gas access to the active site of the Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics
    • Y. Montet, P. Amara, A. Volbeda, X. Vernede, E.C. Hatchikian, and M.J. Field Gas access to the active site of the Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics Nature Struct. Biol. 4 1997 523 526
    • (1997) Nature Struct. Biol. , vol.4 , pp. 523-526
    • Montet, Y.1    Amara, P.2    Volbeda, A.3    Vernede, X.4    Hatchikian, E.C.5    Field, M.J.6
  • 23
    • 0035957218 scopus 로고    scopus 로고
    • Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase
    • D.A. Whittington, A.C. Rosenzweig, C.A. Frederick, and S.J. Lippard Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase Biochemistry 40 2001 3476 3482
    • (2001) Biochemistry , vol.40 , pp. 3476-3482
    • Whittington, D.A.1    Rosenzweig, A.C.2    Frederick, C.A.3    Lippard, S.J.4
  • 24
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structure of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
    • M. Svensson-Ek, J. Abramson, G. Larsson, S. Törnroth, P. Brzezinski, and S. Iwata The X-ray crystal structure of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides J. Mol. Biol. 321 2002 329 339
    • (2002) J. Mol. Biol. , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Törnroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 27
    • 1642534622 scopus 로고    scopus 로고
    • Myoglobin cavities provide interior ligand pathway
    • M.M. Teeter Myoglobin cavities provide interior ligand pathway Protein Sci. 13 2004 313 318
    • (2004) Protein Sci. , vol.13 , pp. 313-318
    • Teeter, M.M.1
  • 28
    • 1842815139 scopus 로고    scopus 로고
    • Kinetic proofreading by the cavity system of myoglobin: Protection from poisoning
    • W. Radding, and G.N. Phillips Kinetic proofreading by the cavity system of myoglobin: protection from poisoning BioEssays 26 2004 422 433
    • (2004) BioEssays , vol.26 , pp. 422-433
    • Radding, W.1    Phillips, G.N.2
  • 29
    • 0031414412 scopus 로고    scopus 로고
    • Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: Implications for the biogenesis of topaquinone
    • M.C.J. Wilce, D.M. Dooley, H.C. Freeman, J.M. Guss, H. Matsunami, and W.S. McIntire Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone Biochemistry 36 1997 16116 16133
    • (1997) Biochemistry , vol.36 , pp. 16116-16133
    • Wilce, M.C.J.1    Dooley, D.M.2    Freeman, H.C.3    Guss, J.M.4    Matsunami, H.5    McIntire, W.S.6
  • 30
    • 0032521219 scopus 로고    scopus 로고
    • Copper amine oxidase from Hansenula polymorpha: The crystal structure determined at 2.4 Å reveals the active conformation
    • R. Li, J.P. Klinman, and F.S. Mathews Copper amine oxidase from Hansenula polymorpha: the crystal structure determined at 2.4 Å reveals the active conformation Structure 6 1998 293 307
    • (1998) Structure , vol.6 , pp. 293-307
    • Li, R.1    Klinman, J.P.2    Mathews, F.S.3
  • 31
    • 0029645871 scopus 로고
    • Crystal structure of a quinoenzyme: Copper amine oxidase of Escherichia coli at 2 Å resolution
    • M.R. Parsons, M.A. Convery, C.M. Wilmot, K.D. Yadav, V. Blakeley, and A.S. Corner Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 Å resolution Structure 3 1995 1171 1184
    • (1995) Structure , vol.3 , pp. 1171-1184
    • Parsons, M.R.1    Convery, M.A.2    Wilmot, C.M.3    Yadav, K.D.4    Blakeley, V.5    Corner, A.S.6
  • 32
  • 33
    • 0033106268 scopus 로고    scopus 로고
    • Remarks about protein structure precision
    • D.W.J. Cruickshank Remarks about protein structure precision Acta Crystallog. sect. D 55 1999 583 601
    • (1999) Acta Crystallog. Sect. D , vol.55 , pp. 583-601
    • Cruickshank, D.W.J.1
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallog. sect. D 53 1997 240 255
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.