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Volumn 292, Issue 11, 2017, Pages 4583-4592

Pre-steady-state kinetics reveal the substrate specificity and mechanism of halide oxidation of truncated human peroxidasin 1

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; ENZYMES; IODINE; OXIDATION; PORPHYRINS; RATE CONSTANTS;

EID: 85015345606     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M117.775213     Document Type: Article
Times cited : (41)

References (38)
  • 2
    • 84902107236 scopus 로고    scopus 로고
    • Bromine is an essential trace element for assembly of collagen IV scaffolds in tissue development and architecture
    • McCall, A. S., Cummings, C. F., Bhave, G., Vanacore, R., Page-McCaw, A., and Hudson, B. G. (2014) Bromine is an essential trace element for assembly of collagen IV scaffolds in tissue development and architecture. Cell 157, 1380-1392
    • (2014) Cell , vol.157 , pp. 1380-1392
    • McCall, A.S.1    Cummings, C.F.2    Bhave, G.3    Vanacore, R.4    Page-McCaw, A.5    Hudson, B.G.6
  • 3
    • 46449130668 scopus 로고    scopus 로고
    • The peroxidase-cyclooxygenase superfamily: Reconstructed evolution of critical enzymes of the innate immune system
    • Zamocky, M., Jakopitsch, C., Furtmüller, P. G., Dunand, C., and Obinger, C. (2008) The peroxidase-cyclooxygenase superfamily: reconstructed evolution of critical enzymes of the innate immune system. Proteins 72, 589-605
    • (2008) Proteins , vol.72 , pp. 589-605
    • Zamocky, M.1    Jakopitsch, C.2    Furtmüller, P.G.3    Dunand, C.4    Obinger, C.5
  • 8
    • 84994793955 scopus 로고    scopus 로고
    • Proprotein convertase processing enhances peroxidasin activity to reinforce collagen IV
    • Colon, S., and Bhave, G. (2016) Proprotein convertase processing enhances peroxidasin activity to reinforce collagen IV. J. Biol. Chem. 291, 24009-24016
    • (2016) J. Biol. Chem. , vol.291 , pp. 24009-24016
    • Colon, S.1    Bhave, G.2
  • 10
    • 84909607969 scopus 로고    scopus 로고
    • How covalent heme to protein bonds influence the formation and reactivity of redox intermediates of a bacterial peroxidase
    • Auer, M., Nicolussi, A., Schütz, G., Furtmüller, P. G., and Obinger, C. (2014) How covalent heme to protein bonds influence the formation and reactivity of redox intermediates of a bacterial peroxidase. J. Biol. Chem. 289, 31480-31491
    • (2014) J. Biol. Chem. , vol.289 , pp. 31480-31491
    • Auer, M.1    Nicolussi, A.2    Schütz, G.3    Furtmüller, P.G.4    Obinger, C.5
  • 12
    • 0021139728 scopus 로고
    • A kinetic study of the reaction between human myeloperoxidase, hydroperoxides and cyanide. Inhibition by chloride and thiocyanate
    • Bolscher, B. G., and Wever, R. (1984) A kinetic study of the reaction between human myeloperoxidase, hydroperoxides and cyanide. Inhibition by chloride and thiocyanate. Biochim. Biophys. Acta 788, 1-10
    • (1984) Biochim. Biophys. Acta , vol.788 , pp. 1-10
    • Bolscher, B.G.1    Wever, R.2
  • 15
    • 56349167084 scopus 로고    scopus 로고
    • Identification and characterization of VPO1, a new animal heme-containing peroxidase
    • Cheng, G., Salerno, J. C., Cao, Z., Pagano, P. J., and Lambeth, J. D. (2008) Identification and characterization of VPO1, a new animal heme-containing peroxidase. Free Radic. Biol. Med. 45, 1682-1694
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 1682-1694
    • Cheng, G.1    Salerno, J.C.2    Cao, Z.3    Pagano, P.J.4    Lambeth, J.D.5
  • 16
    • 79958836580 scopus 로고    scopus 로고
    • Involvement of vascular peroxidase 1 in angiotensin II-induced vascular smooth muscle cell proliferation
    • Shi, R., Hu, C., Yuan, Q., Yang, T., Peng, J., Li, Y., Bai, Y., Cao, Z., Cheng, G., and Zhang, G. (2011) Involvement of vascular peroxidase 1 in angiotensin II-induced vascular smooth muscle cell proliferation. Cardiovasc. Res. 91, 27-36
    • (2011) Cardiovasc. Res. , vol.91 , pp. 27-36
    • Shi, R.1    Hu, C.2    Yuan, Q.3    Yang, T.4    Peng, J.5    Li, Y.6    Bai, Y.7    Cao, Z.8    Cheng, G.9    Zhang, G.10
  • 17
    • 84940557304 scopus 로고    scopus 로고
    • The ancient immunoglobulin domains of peroxidasin are required to form sulfilimine cross-links in collagen IV
    • Ero-Tolliver, I. A., Hudson, B. G., and Bhave, G. (2015) The ancient immunoglobulin domains of peroxidasin are required to form sulfilimine cross-links in collagen IV. J. Biol. Chem. 290, 21741-21748
    • (2015) J. Biol. Chem. , vol.290 , pp. 21741-21748
    • Ero-Tolliver, I.A.1    Hudson, B.G.2    Bhave, G.3
  • 18
    • 34249809407 scopus 로고    scopus 로고
    • Heme to protein linkages in mammalian peroxidases: Impact on spectroscopic, redox and catalytic properties
    • Zederbauer, M., Furtmüller, P. G., Brogioni, S., Jakopitsch, C., Smulevich, G., and Obinger, C. (2007) Heme to protein linkages in mammalian peroxidases: impact on spectroscopic, redox and catalytic properties. Nat. Prod. Rep. 24, 571-584
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 571-584
    • Zederbauer, M.1    Furtmüller, P.G.2    Brogioni, S.3    Jakopitsch, C.4    Smulevich, G.5    Obinger, C.6
  • 19
    • 41949113795 scopus 로고    scopus 로고
    • The role of the sulfonium ion linkage in the stabilization of the heme architecture of the ferrous form of myeloperoxidase: A comparison with lactoperoxidase
    • Brogioni, S., Stampler, J., Furtmüller, P. G., Feis, A., Obinger, C., and Smulevich, G. (2008) The role of the sulfonium ion linkage in the stabilization of the heme architecture of the ferrous form of myeloperoxidase: a comparison with lactoperoxidase. Biochim. Biophys. Acta 1784, 843-849
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 843-849
    • Brogioni, S.1    Stampler, J.2    Furtmüller, P.G.3    Feis, A.4    Obinger, C.5    Smulevich, G.6
  • 22
    • 0030910381 scopus 로고    scopus 로고
    • Autocatalytic processing of heme lactoperoxidase produces the native protein-bound prosthetic group
    • DePillis, G. D., Ozaki Si, Kuo, J. M., Maltby, D. A., and Ortiz de Montellano, P. R. (1997) Autocatalytic processing of heme lactoperoxidase produces the native protein-bound prosthetic group. J. Biol. Chem. 272, 8857-8860
    • (1997) J. Biol. Chem. , vol.272 , pp. 8857-8860
    • DePillis, G.D.1    Si, O.2    Kuo, J.M.3    Maltby, D.A.4    Ortiz De Montellano, P.R.5
  • 23
    • 0033537889 scopus 로고    scopus 로고
    • 2 generated at the apical surface of thyroid cells in autocatalytic covalent heme binding
    • 2 generated at the apical surface of thyroid cells in autocatalytic covalent heme binding. J. Biol. Chem. 274, 10533-10538
    • (1999) J. Biol. Chem. , vol.274 , pp. 10533-10538
    • Fayadat, L.1    Niccoli-Sire, P.2    Lanet, J.3    Franc, J.L.4
  • 24
    • 47649104479 scopus 로고    scopus 로고
    • Mechanism and role of covalent heme binding in the CYP4 family of P450 enzymes and the mammalian peroxidases
    • Ortiz de Montellano, P. R. (2008) Mechanism and role of covalent heme binding in the CYP4 family of P450 enzymes and the mammalian peroxidases. Drug Metab. Rev. 40, 405-426
    • (2008) Drug Metab. Rev. , vol.40 , pp. 405-426
    • Ortiz De Montellano, P.R.1
  • 25
    • 34447117575 scopus 로고    scopus 로고
    • Disruption of the aspartate to heme ester linkage in human myeloperoxidase: Impact on ligand binding, redox chemistry and interconversion of redox intermediates
    • Zederbauer, M., Furtmüller, P. G., Bellei, M., Stampler, J., Jakopitsch, C., Battistuzzi, G., Moguilevsky, N., and Obinger, C. (2007) Disruption of the aspartate to heme ester linkage in human myeloperoxidase: impact on ligand binding, redox chemistry and interconversion of redox intermediates. J. Biol. Chem. 282, 17041-17052
    • (2007) J. Biol. Chem. , vol.282 , pp. 17041-17052
    • Zederbauer, M.1    Furtmüller, P.G.2    Bellei, M.3    Stampler, J.4    Jakopitsch, C.5    Battistuzzi, G.6    Moguilevsky, N.7    Obinger, C.8
  • 26
    • 33947405315 scopus 로고    scopus 로고
    • Manipulating the vinyl-sulfonium bond in human myeloperoxidase: Impact on compound I formation and reduction by halides and thiocyanate
    • Zederbauer, M., Furtmüller, P. G., Ganster, B., Moguilevsky, N., and Obinger, C. (2007) Manipulating the vinyl-sulfonium bond in human myeloperoxidase: impact on compound I formation and reduction by halides and thiocyanate. Biochem. Biophys. Res. Commun. 356, 450-456
    • (2007) Biochem. Biophys. Res. Commun. , vol.356 , pp. 450-456
    • Zederbauer, M.1    Furtmüller, P.G.2    Ganster, B.3    Moguilevsky, N.4    Obinger, C.5
  • 28
    • 85008233999 scopus 로고    scopus 로고
    • Structure of bovine lactoperoxidase with a partially linked heme moiety at 1.98 Å resolution
    • Singh, P. K., Sirohi, H. V., Iqbal, N., Tiwari, P., Kaur, P., Sharma, S., and Singh, T. P. (2017) Structure of bovine lactoperoxidase with a partially linked heme moiety at 1.98 Å resolution. Biochim. Biophys. Acta 1865, 329-335
    • (2017) Biochim. Biophys. Acta , vol.1865 , pp. 329-335
    • Singh, P.K.1    Sirohi, H.V.2    Iqbal, N.3    Tiwari, P.4    Kaur, P.5    Sharma, S.6    Singh, T.P.7
  • 29
    • 33750346770 scopus 로고    scopus 로고
    • Redox thermodynamics of the Fe(III)/Fe(II) couple of human myeloperoxidase in its high-spin and low-spin forms
    • Battistuzzi, G., Bellei, M., Zederbauer, M., Furtmüller, P. G., Sola, M., and Obinger, C. (2006) Redox thermodynamics of the Fe(III)/Fe(II) couple of human myeloperoxidase in its high-spin and low-spin forms. Biochemistry 45, 12750-12755
    • (2006) Biochemistry , vol.45 , pp. 12750-12755
    • Battistuzzi, G.1    Bellei, M.2    Zederbauer, M.3    Furtmüller, P.G.4    Sola, M.5    Obinger, C.6
  • 30
    • 0032558979 scopus 로고    scopus 로고
    • Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate
    • Furtmüller, P. G., Burner, U., and Obinger, C. (1998) Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate. Biochemistry 37, 17923-17930
    • (1998) Biochemistry , vol.37 , pp. 17923-17930
    • Furtmüller, P.G.1    Burner, U.2    Obinger, C.3
  • 31
    • 0034687654 scopus 로고    scopus 로고
    • Spectral and kinetic studies on the formation of eosinophil peroxidase compound I and its reaction with halides and thiocyanate
    • Furtmüller, P. G., Burner, U., Regelsberger, G., and Obinger, C. (2000) Spectral and kinetic studies on the formation of eosinophil peroxidase compound I and its reaction with halides and thiocyanate. Biochemistry 39, 15578-15584
    • (2000) Biochemistry , vol.39 , pp. 15578-15584
    • Furtmüller, P.G.1    Burner, U.2    Regelsberger, G.3    Obinger, C.4
  • 32
    • 30544439048 scopus 로고    scopus 로고
    • Structural and functional aspects of thyroid peroxidase
    • Ruf, J., and Carayon, P. (2006) Structural and functional aspects of thyroid peroxidase. Arch. Biochem. Biophys. 445, 269-277
    • (2006) Arch. Biochem. Biophys. , vol.445 , pp. 269-277
    • Ruf, J.1    Carayon, P.2
  • 34
    • 0033769965 scopus 로고    scopus 로고
    • Cyanide and thiocyanate levels in blood and saliva of healthy adult volunteers
    • Tsuge, K., Kataoka, M., and Seto, Y. (2000) Cyanide and thiocyanate levels in blood and saliva of healthy adult volunteers. J. Health Sci. 46, 343-350
    • (2000) J. Health Sci. , vol.46 , pp. 343-350
    • Tsuge, K.1    Kataoka, M.2    Seto, Y.3
  • 35
    • 0018647425 scopus 로고
    • Fetal cardiovascular system as influenced by maternal smoking
    • Asmussen, I. (1979) Fetal cardiovascular system as influenced by maternal smoking. Clin. Cardiol. 2, 246-256
    • (1979) Clin. Cardiol. , vol.2 , pp. 246-256
    • Asmussen, I.1
  • 36
    • 70449679220 scopus 로고    scopus 로고
    • The role of hypothiocyanous acid (HOSCN) in biological systems
    • Hawkins, C. L. (2009) The role of hypothiocyanous acid (HOSCN) in biological systems. Free Radic. Res. 43, 1147-1158
    • (2009) Free Radic. Res. , vol.43 , pp. 1147-1158
    • Hawkins, C.L.1
  • 37
    • 77955474149 scopus 로고    scopus 로고
    • The myeloperoxidase-derived oxidant HOSCN inhibits protein tyrosine phosphatases and modulates cell signaling via the mitogen-activated protein kinase (MAPK) pathway in macrophages
    • Lane, A. E., Tan, J. T., Hawkins, C. L., Heather, A. K., and Davies, M. J. (2010) The myeloperoxidase-derived oxidant HOSCN inhibits protein tyrosine phosphatases and modulates cell signaling via the mitogen-activated protein kinase (MAPK) pathway in macrophages. Biochem. J. 430, 161-169
    • (2010) Biochem. J. , vol.430 , pp. 161-169
    • Lane, A.E.1    Tan, J.T.2    Hawkins, C.L.3    Heather, A.K.4    Davies, M.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.