메뉴 건너뛰기




Volumn 45, Issue 37, 2006, Pages 11140-11150

pH dependence of peptidylglycine monooxygenase. Mechanistic implications of Cu-methionine binding dynamics

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION SPECTROSCOPY; CATALYSIS; CHEMICAL BONDS; COMPUTER SIMULATION; CONFORMATIONS; MATHEMATICAL MODELS; PH EFFECTS; X RAY ANALYSIS;

EID: 33748775782     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060905a     Document Type: Article
Times cited : (19)

References (46)
  • 1
    • 7744231498 scopus 로고    scopus 로고
    • Mechanisms whereby mononuclear copper proteins functionalize organic substrates
    • Klinman, J. P. (1996) Mechanisms whereby mononuclear copper proteins functionalize organic substrates, Chem. Rev. 96, 2541-2561.
    • (1996) Chem. Rev. , vol.96 , pp. 2541-2561
    • Klinman, J.P.1
  • 2
    • 0000821179 scopus 로고    scopus 로고
    • New insights into copper monooxygenases and peptide amidation: Structure, mechanism and function
    • Prigge, S. T., Mains, R. E., Eipper, B. A., and Amzel, L. M. (2000) New insights into copper monooxygenases and peptide amidation: Structure, mechanism and function, Cell. Mol. Life Sci. 57, 1236-1259.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1236-1259
    • Prigge, S.T.1    Mains, R.E.2    Eipper, B.A.3    Amzel, L.M.4
  • 3
    • 33645637817 scopus 로고    scopus 로고
    • The copper-enzyme family of dopamine β-monooxygenase and peptidylglycine α-hydroxylating monooxygenase: Resolving the chemical pathway for substrate hydroxylation
    • Klinman, J. P. (2006) The copper-enzyme family of dopamine β-monooxygenase and peptidylglycine α-hydroxylating monooxygenase: Resolving the chemical pathway for substrate hydroxylation, J. Biol. Chem. 281, 3013-3016.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3013-3016
    • Klinman, J.P.1
  • 4
    • 0030699146 scopus 로고    scopus 로고
    • Amidation of bioactive peptides: The structure of peptidylglycine α-hydroxylating monooxygenase
    • Prigge, S. T., Kolhekar, A. S., Eipper, B. A., Mains, R. E., and Amzel, L. M. (1997) Amidation of bioactive peptides: The structure of peptidylglycine α-hydroxylating monooxygenase, Science 278, 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
  • 5
    • 0032861557 scopus 로고    scopus 로고
    • Substrate-mediated electron transfer in peptidylglycine α-hydroxylating monooxygenase
    • Prigge, S. T., Kolhekar, A. S., Eipper, B. A., Mains, R. E., and Amzel, L. M. (1999) Substrate-mediated electron transfer in peptidylglycine α-hydroxylating monooxygenase, Nat. Struct. Biol. 6, 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
  • 6
    • 2442545587 scopus 로고    scopus 로고
    • Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex
    • Prigge, S. T., Eipper, B. A., Mains, R. E., and Amzel, M. (2004) Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex, Science 304, 864-867.
    • (2004) Science , vol.304 , pp. 864-867
    • Prigge, S.T.1    Eipper, B.A.2    Mains, R.E.3    Amzel, M.4
  • 7
    • 27744459340 scopus 로고    scopus 로고
    • The catalytic copper of peptidylglycine α-hydroxylating monooxygenase also plays a critical structural role
    • Siebert, X., Eipper, B. A., Mains, R. E., Prigge, S. T., Blackburn, N. J., and Amzel, L. M. (2005) The catalytic copper of peptidylglycine α-hydroxylating monooxygenase also plays a critical structural role, Biophys. J. 89, 3312-3319.
    • (2005) Biophys. J. , vol.89 , pp. 3312-3319
    • Siebert, X.1    Eipper, B.A.2    Mains, R.E.3    Prigge, S.T.4    Blackburn, N.J.5    Amzel, L.M.6
  • 8
    • 0029739477 scopus 로고    scopus 로고
    • Structural investigations on the coordination environment of the active-site copper centers of recombinant bifunctional peptidylglycine α-amidating enzyme
    • Boswell, J. S., Reedy, B. J., Kulathila, R., Merkler, D. J., and Blackburn, N. J. (1996) Structural investigations on the coordination environment of the active-site copper centers of recombinant bifunctional peptidylglycine α-amidating enzyme, Biochemistry 35, 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
  • 9
    • 0030766385 scopus 로고    scopus 로고
    • Peptidylglycine α-hydroxylating monooxygenase: Active site residues, disulfide linkages, and a two-domain model of the catalytuc core
    • Kolhekar, A. S., Keutman, H. T., Mains, R. E., Quon, A. S. W., and Eipper, B. A. (1997) Peptidylglycine α-hydroxylating monooxygenase: Active site residues, disulfide linkages, and a two-domain model of the catalytuc core, Biochemistry 36, 10901-10909.
    • (1997) Biochemistry , vol.36 , pp. 10901-10909
    • Kolhekar, A.S.1    Keutman, H.T.2    Mains, R.E.3    Quon, A.S.W.4    Eipper, B.A.5
  • 10
    • 0033576285 scopus 로고    scopus 로고
    • Does superoxide channel between the copper centers in peptidylglycine monooxygenase? A new mechanism based on carbon monoxide reactivity
    • Jaron, S., and Blackburn, N. J. (1999) Does superoxide channel between the copper centers in peptidylglycine monooxygenase? A new mechanism based on carbon monoxide reactivity, Biochemistry 38, 15086-15096.
    • (1999) Biochemistry , vol.38 , pp. 15086-15096
    • Jaron, S.1    Blackburn, N.J.2
  • 11
    • 0034123872 scopus 로고    scopus 로고
    • Major changes in copper coordination accompany reduction of peptidylglycine monooxygenase
    • Blackburn, N. J., Rhames, F. C., Ralle, M., and Jaron, S. (2000) Major changes in copper coordination accompany reduction of peptidylglycine monooxygenase, J. Biol. Inorg. Chem. 5, 341-353.
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 341-353
    • Blackburn, N.J.1    Rhames, F.C.2    Ralle, M.3    Jaron, S.4
  • 12
    • 0035849535 scopus 로고    scopus 로고
    • Characterization of a half-apo derivative of peptidylglycine monooxygenase. Insight into the reactivity of each active site copper
    • Jaron, S., and Blackburn, N. J. (2001) Characterization of a half-apo derivative of peptidylglycine monooxygenase. Insight into the reactivity of each active site copper, Biochemistry 40, 6867-6875.
    • (2001) Biochemistry , vol.40 , pp. 6867-6875
    • Jaron, S.1    Blackburn, N.J.2
  • 13
    • 0037027322 scopus 로고    scopus 로고
    • The catalytic role of the copper ligand H172 of peptidylglycine α-hydroxylating monooxygenase (PHM): A spectroscopic study of the H172A mutant
    • Jaron, S., Mains, R. E., Eipper, B. A., and Blackburn, N. J. (2002) The catalytic role of the copper ligand H172 of peptidylglycine α- hydroxylating monooxygenase (PHM): A spectroscopic study of the H172A mutant, Biochemistry 41, 13274-13282.
    • (2002) Biochemistry , vol.41 , pp. 13274-13282
    • Jaron, S.1    Mains, R.E.2    Eipper, B.A.3    Blackburn, N.J.4
  • 14
    • 0037793356 scopus 로고    scopus 로고
    • Mechanistic investigation of peptidylglycine α-hydroxylating monooxygenase via intrinsic tryptophan fluorescence and mutagenesis
    • Bell, J., El Meskini, R., D'Amato, D., Mains, R. E., and Eipper, B. A. (2003) Mechanistic investigation of peptidylglycine α-hydroxylating monooxygenase via intrinsic tryptophan fluorescence and mutagenesis, Biochemistry 42, 7133-7142.
    • (2003) Biochemistry , vol.42 , pp. 7133-7142
    • Bell, J.1    El Meskini, R.2    D'Amato, D.3    Mains, R.E.4    Eipper, B.A.5
  • 16
    • 0346118953 scopus 로고    scopus 로고
    • Evidence that dioxygen and substrate activation are tightly coupled in dopamine β-monooxygenase: Implications for oxygen activation
    • Evans, J. P., Ahn, K., and Klinman, J. P. (2003) Evidence that dioxygen and substrate activation are tightly coupled in dopamine β-monooxygenase: Implications for oxygen activation, J. Biol. Chem. 278, 49691-49698.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49691-49698
    • Evans, J.P.1    Ahn, K.2    Klinman, J.P.3
  • 17
    • 0032474461 scopus 로고    scopus 로고
    • Kinetic mechanism and intrinsic isotope effects for the peptidylglycine α-amidating enzyme reaction
    • Francisco, W. A., Merkler, D. J., Blackburn, N. J., and Klinman, J. P. (1998) Kinetic mechanism and intrinsic isotope effects for the peptidylglycine α-amidating enzyme reaction, Biochemistry 37, 8244-8252.
    • (1998) Biochemistry , vol.37 , pp. 8244-8252
    • Francisco, W.A.1    Merkler, D.J.2    Blackburn, N.J.3    Klinman, J.P.4
  • 18
    • 0037125529 scopus 로고    scopus 로고
    • Hydrogen tunneling in peptidylglycine α-hydroxylating monooxygenase
    • Francisco, W. A., Knapp, M. J., Blackburn, N. J., and Klinman, J. P. (2002) Hydrogen tunneling in peptidylglycine α-hydroxylating monooxygenase, J. Am. Chem. Soc. 124, 8194-8195.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 8194-8195
    • Francisco, W.A.1    Knapp, M.J.2    Blackburn, N.J.3    Klinman, J.P.4
  • 19
    • 0345270446 scopus 로고    scopus 로고
    • Oxygen and hydrogen isotope effects in an active site tyrosine to phenylalanine mutant of peptidylglycine α-hydroxylating monooxygenase: Mechanistic implications
    • Francisco, W. A., Blackburn, N. J., and Klinman, J. P. (2003) Oxygen and hydrogen isotope effects in an active site tyrosine to phenylalanine mutant of peptidylglycine α-hydroxylating monooxygenase: Mechanistic implications, Biochemistry 42, 1813-1819.
    • (2003) Biochemistry , vol.42 , pp. 1813-1819
    • Francisco, W.A.1    Blackburn, N.J.2    Klinman, J.P.3
  • 20
    • 6044235540 scopus 로고    scopus 로고
    • Investigation of the pathway for inter-copper electron transfer in peptidylglycine α-amidating monooxygenase
    • Francisco, W. A., Wille, G., Smith, A. J., Merkler, D. J., and Klinman, J. P. (2004) Investigation of the pathway for inter-copper electron transfer in peptidylglycine α-amidating monooxygenase, J. Am. Chem. Soc. 126, 13168-13169.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 13168-13169
    • Francisco, W.A.1    Wille, G.2    Smith, A.J.3    Merkler, D.J.4    Klinman, J.P.5
  • 23
    • 0037389858 scopus 로고    scopus 로고
    • A redox switch in CopC: An intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites
    • Arnesano, F., Banci, L., Bertini, I., Mangani, S., and Thompsett, A. R. (2003) A redox switch in CopC: An intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites, Proc. Natl. Acad. Sci. U.S.A. 100, 3814-3819.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3814-3819
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Mangani, S.4    Thompsett, A.R.5
  • 24
    • 0037438520 scopus 로고    scopus 로고
    • The PcoC copper resistance protein coordinates Cu(I) via novel S-methionine interactions
    • Peariso, K., Huffman, D. L., Penner-Hahn, J. E., and O'Halloran, T. V. (2003) The PcoC copper resistance protein coordinates Cu(I) via novel S-methionine interactions, J. Am. Chem. Soc. 125, 342-343.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 342-343
    • Peariso, K.1    Huffman, D.L.2    Penner-Hahn, J.E.3    O'Halloran, T.V.4
  • 25
    • 0037260040 scopus 로고    scopus 로고
    • Crystal structure and dimerization equilibria of PcoC, a methionine-rich copper resistance protein from Escherichia coli
    • Wernimont, A. K., Huffman, D. L., Finney, L. A., Demeler, B., O'Halloran, T. V., and Rosenzweig, A. C. (2003) Crystal structure and dimerization equilibria of PcoC, a methionine-rich copper resistance protein from Escherichia coli, J. Biol. Inorg. Chem. 8, 185-194.
    • (2003) J. Biol. Inorg. Chem. , vol.8 , pp. 185-194
    • Wernimont, A.K.1    Huffman, D.L.2    Finney, L.A.3    Demeler, B.4    O'Halloran, T.V.5    Rosenzweig, A.C.6
  • 26
    • 1942504122 scopus 로고    scopus 로고
    • Oxygen activation by the noncoupled binuclear copper site in peptidylglycine α-hydroxylating monooxygenase. Reaction mechanism and role of the noncoupled nature of the active site
    • Chen, P., and Solomon, E. I. (2004) Oxygen activation by the noncoupled binuclear copper site in peptidylglycine α-hydroxylating monooxygenase. Reaction mechanism and role of the noncoupled nature of the active site, J. Am. Chem. Soc. 126, 4991-5000.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4991-5000
    • Chen, P.1    Solomon, E.I.2
  • 27
    • 0036009142 scopus 로고    scopus 로고
    • The crystal structure of catechol oxidase: New insight into the function of type-3 copper proteins
    • Gerdemann, C., Eicken, C., and Krebs, B. (2002) The crystal structure of catechol oxidase: New insight into the function of type-3 copper proteins, Acc. Chem. Res. 35, 183-191.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 183-191
    • Gerdemann, C.1    Eicken, C.2    Krebs, B.3
  • 28
    • 4544332259 scopus 로고    scopus 로고
    • 2 activation by binuclear Cu sites: Noncoupled versus exchange coupled reaction mechanisms
    • 2 activation by binuclear Cu sites: Noncoupled versus exchange coupled reaction mechanisms, Proc. Natl. Acad. Sci. U.S.A. 101, 13105-13110.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 13105-13110
    • Chen, P.1    Solomon, E.I.2
  • 29
    • 33645219172 scopus 로고    scopus 로고
    • The hydrogen peroxide reactivity of peptidylglycine monooxygenase supports a Cu(II)-superoxo catalytic intermediate
    • Bauman, A. T., Yukl, E. T., Alkevich, K., McCormack, A. L., and Blackburn, N. J. (2006) The hydrogen peroxide reactivity of peptidylglycine monooxygenase supports a Cu(II)-superoxo catalytic intermediate, J. Biol. Chem. 281, 4190-4198.
    • (2006) J. Biol. Chem. , vol.281 , pp. 4190-4198
    • Bauman, A.T.1    Yukl, E.T.2    Alkevich, K.3    McCormack, A.L.4    Blackburn, N.J.5
  • 30
    • 20744452335 scopus 로고    scopus 로고
    • Computational exploration of the catalytic mechanism of dopamine β-monooxygenase: Modeling of its mononuclear copper active sites
    • Kamachi, T., Kihara, N., Shiota, Y., and Yoshizawa, K. (2005) Computational exploration of the catalytic mechanism of dopamine β-monooxygenase: Modeling of its mononuclear copper active sites, Inorg. Chem. 44, 4226-4236.
    • (2005) Inorg. Chem. , vol.44 , pp. 4226-4236
    • Kamachi, T.1    Kihara, N.2    Shiota, Y.3    Yoshizawa, K.4
  • 31
    • 0028913562 scopus 로고
    • The catalytic core of peptidylglycine α-hydroxylating monooxygenase: Investigation by site-directed mutagenesis, Cu X-ray absorption spectroscopy, and electron paramagnetic resonance
    • Eipper, B. A., Quon, A. S. W., Mains, R. E., Boswell, J. S., and Blackburn, N. J. (1995) The catalytic core of peptidylglycine α-hydroxylating monooxygenase: Investigation by site-directed mutagenesis, Cu X-ray absorption spectroscopy, and electron paramagnetic resonance, Biochemistry 34, 2857-2865.
    • (1995) Biochemistry , vol.34 , pp. 2857-2865
    • Eipper, B.A.1    Quon, A.S.W.2    Mains, R.E.3    Boswell, J.S.4    Blackburn, N.J.5
  • 32
    • 0003795626 scopus 로고
    • Stanford Synchrotron Radiation Laboratory, Menlo Park, CA
    • George, G. N. (1990) EXAFSPAK, Stanford Synchrotron Radiation Laboratory, Menlo Park, CA.
    • (1990) EXAFSPAK
    • George, G.N.1
  • 34
    • 35548993600 scopus 로고
    • A rapid, exact, curved-wave theory for EXAFS calculations
    • Gurman, S. J., Binsted, N., and Ross, I. (1984) A rapid, exact, curved-wave theory for EXAFS calculations, J. Phys. C 17, 143-151.
    • (1984) J. Phys. C , vol.17 , pp. 143-151
    • Gurman, S.J.1    Binsted, N.2    Ross, I.3
  • 35
    • 33744602646 scopus 로고
    • A rapid, exact, curved-wave theory for EXAFS calculations. II. The multiple-scattering contributions
    • Gurman, S. J., Binsted, N., and Ross, I. (1986) A rapid, exact, curved-wave theory for EXAFS calculations. II. The multiple-scattering contributions, J. Phys. C 19, 1845-1861.
    • (1986) J. Phys. C , vol.19 , pp. 1845-1861
    • Gurman, S.J.1    Binsted, N.2    Ross, I.3
  • 36
    • 9644277158 scopus 로고    scopus 로고
    • State of the art analysis of whole X-ray absorption spectra
    • Binsted, N., and Hasnain, S. S. (1996) State of the art analysis of whole X-ray absorption spectra, J. Synchrotron Radiat. 3, 185-196.
    • (1996) J. Synchrotron Radiat. , vol.3 , pp. 185-196
    • Binsted, N.1    Hasnain, S.S.2
  • 37
    • 0001079697 scopus 로고
    • Chemistry and structural studies on the dioxygen-binding copper 1,2-dimethylimidazole system
    • Sanyal, I., Karlin, K. D., Strange, R. W., and Blackburn, N. J. (1993) Chemistry and structural studies on the dioxygen-binding copper 1,2-dimethylimidazole system, J. Am. Chem. Soc. 115, 11259-11270.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 11259-11270
    • Sanyal, I.1    Karlin, K.D.2    Strange, R.W.3    Blackburn, N.J.4
  • 38
    • 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., Penner-Hahn, J. E., Hodgson, K. O., and Solomon, E. I. (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, 6433-6422.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 6433-16422
    • Kau, L.S.1    Spira-Solomon, D.2    Penner-Hahn, J.E.3    Hodgson, K.O.4    Solomon, E.I.5
  • 39
    • 0001369913 scopus 로고
    • X-ray absorption edge spectroscopy of copper(I) complexes. Coordination geometry of copper(I) in the reduced forms of copper proteins and their derivatives with carbon monoxide
    • Blackburn, N. J., Strange, R. W., Reedijk, J., Volbeda, A., Farooq, A., Karlin, K. D., and Zubieta, J. (1989) X-ray absorption edge spectroscopy of copper(I) complexes. Coordination geometry of copper(I) in the reduced forms of copper proteins and their derivatives with carbon monoxide, Inorg. Chem. 28, 1349-1357.
    • (1989) Inorg. Chem. , vol.28 , pp. 1349-1357
    • Blackburn, N.J.1    Strange, R.W.2    Reedijk, J.3    Volbeda, A.4    Farooq, A.5    Karlin, K.D.6    Zubieta, J.7
  • 40
    • 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., and Shigeta, R. T. (1990) Characterization of a carbon monoxide complex of reduced dopamine-β-hydroxylase: Evidence for inequivalence of the Cu(I) centers, J. Biol. Chem. 265, 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
  • 41
    • 0026012433 scopus 로고
    • Carbonmonoxy dopamine-β-hydroxylase: Structural characterization by FTIR, fluorescence and XAS spectroscopy
    • Pettingill, T. M., Strange, R. W., and Blackburn, N. J. (1991) Carbonmonoxy dopamine-β-hydroxylase: Structural characterization by FTIR, fluorescence and XAS spectroscopy, J. Biol. Chem. 266, 16996-17003.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16996-17003
    • Pettingill, T.M.1    Strange, R.W.2    Blackburn, N.J.3
  • 42
    • 0000211556 scopus 로고
    • Absorption, emission, and photophysical properties of copper(I) pyrazole complexes and their carbonyl adducts
    • Sorrell, T. N., and Borovick, A. S. (1987) Absorption, emission, and photophysical properties of copper(I) pyrazole complexes and their carbonyl adducts, Inorg. Chem. 26, 1957-1964.
    • (1987) Inorg. Chem. , vol.26 , pp. 1957-1964
    • Sorrell, T.N.1    Borovick, A.S.2
  • 45
    • 0036301901 scopus 로고    scopus 로고
    • Environmentally coupled hydrogen tunneling. Linking catalysis to dynamics
    • Knapp, M. J., and Klinman, J. P. (2002) Environmentally coupled hydrogen tunneling. Linking catalysis to dynamics, Eur. J. Biochem. 269, 3113-3121.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3113-3121
    • Knapp, M.J.1    Klinman, J.P.2
  • 46
    • 33748902041 scopus 로고    scopus 로고
    • The role of tunneling in enzyme catalysis of C-H activation
    • in press
    • Klinman, J. P. (2006) The role of tunneling in enzyme catalysis of C-H activation, Biochim. Biophys. Acta (in press).
    • (2006) Biochim. Biophys. Acta
    • Klinman, J.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.