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Volumn 40, Issue 3, 2005, Pages 325-330

Characterization of a novel microperoxidase from Marinobacter hydrocarbonoclasticus by electrospray ionization tandem mass spectrometry

Author keywords

Cytochrome c; Electrospray ionization tandem mass spectrometry; Heme cofactor; Microperoxidase

Indexed keywords

AMINO ACIDS; CHEMICAL BONDS; IONIZATION; IRON; MASS SPECTROMETRY; REDUCTION; SOLUBILITY;

EID: 15444364433     PISSN: 10765174     EISSN: None     Source Type: Journal    
DOI: 10.1002/jms.788     Document Type: Article
Times cited : (4)

References (31)
  • 1
  • 2
    • 0022760446 scopus 로고
    • Hemes and hemoproteins, 1: Preparation and analysis of the heme-containing octapeptide (microperoxidase-8) and identification of the monomeric form in aqueous solution
    • Aron J, Baldwin DA, Marques HM, Pratt JM, Adams PA. Hemes and hemoproteins, 1: preparation and analysis of the heme-containing octapeptide (microperoxidase-8) and identification of the monomeric form in aqueous solution. J. Inorg. Biochem. 1986; 27: 227.
    • (1986) J. Inorg. Biochem. , vol.27 , pp. 227
    • Aron, J.1    Baldwin, D.A.2    Marques, H.M.3    Pratt, J.M.4    Adams, P.A.5
  • 3
    • 0023369081 scopus 로고
    • Hemes and hemoproteins, 5: Kinetics of the peroxidatic activity of microperoxidase-8: Model for the peroxidase enzymes
    • Baldwin DA, Marques HM, Pratt JM. Hemes and hemoproteins, 5: kinetics of the peroxidatic activity of microperoxidase-8: model for the peroxidase enzymes. J. Inorg. Biochem. 1987; 30: 203.
    • (1987) J. Inorg. Biochem. , vol.30 , pp. 203
    • Baldwin, D.A.1    Marques, H.M.2    Pratt, J.M.3
  • 4
    • 0024464521 scopus 로고
    • Kinetics of heme octapeptide (microperoxidase-8) formation studied by high-pressure liquid chromatography (HPLC) monitoring of the peptic and tryptic hydrolysis of horse heart cytochrome-c
    • Adams PA, Byfield MP, Goold RD, Thumser AE. Kinetics of heme octapeptide (microperoxidase-8) formation studied by high-pressure liquid chromatography (HPLC) monitoring of the peptic and tryptic hydrolysis of horse heart cytochrome-c. J. Inorg. Biochem. 1989; 37: 55.
    • (1989) J. Inorg. Biochem. , vol.37 , pp. 55
    • Adams, P.A.1    Byfield, M.P.2    Goold, R.D.3    Thumser, A.E.4
  • 5
    • 0031056633 scopus 로고    scopus 로고
    • Paramagnetic NMR spectroscopy of microperoxidase-8
    • Low DW, Gray HB, Duus JØ. Paramagnetic NMR spectroscopy of microperoxidase-8. J. Am. Chem. Soc. 1997; 119: 1.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 1
    • Low, D.W.1    Gray, H.B.2    Duus, J.Ø.3
  • 10
    • 0034830870 scopus 로고    scopus 로고
    • Microperoxidase-8 catalyzed nitration of phenol by nitrogen dioxide radicals
    • Ricoux R, Boucher JL, Mansuy D, Mahy JP. Microperoxidase-8 catalyzed nitration of phenol by nitrogen dioxide radicals. Eur. J. Biochem. 2001; 268: 3783.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3783
    • Ricoux, R.1    Boucher, J.L.2    Mansuy, D.3    Mahy, J.P.4
  • 11
    • 0014913803 scopus 로고
    • A heme-peptide as an ultrastructural tracer
    • Feder N. A heme-peptide as an ultrastructural tracer. J. Histochem. Cytochem. 1970; 18: 911.
    • (1970) J. Histochem. Cytochem. , vol.18 , pp. 911
    • Feder, N.1
  • 12
    • 0021908790 scopus 로고
    • Anionized and cationized hemeundecapeptides as probes for cell surface charge and permeability studies: Differentiated labeling of endothelial plasmalemmal vesicles
    • Ghinea N, Simionescu N. Anionized and cationized hemeundecapeptides as probes for cell surface charge and permeability studies: differentiated labeling of endothelial plasmalemmal vesicles. J. Cell. Biol. 1985; 100: 606.
    • (1985) J. Cell. Biol. , vol.100 , pp. 606
    • Ghinea, N.1    Simionescu, N.2
  • 13
    • 0031152306 scopus 로고    scopus 로고
    • Microperoxidase-11-mediated reduction of hemoproteins: Electrocatalyzed reduction of cytochrome c, myoglobin and hemoglobin and electrocatalytic reduction of nitrate in the presence of cytochrome-dependent nitrate reductase
    • Narvaez A, Dominguez E, Katakis I, Katz E, Ranjit KT, Ben-Dov I, Willner I. Microperoxidase-11-mediated reduction of hemoproteins: electrocatalyzed reduction of cytochrome c, myoglobin and hemoglobin and electrocatalytic reduction of nitrate in the presence of cytochrome-dependent nitrate reductase. J. Electroanal. Chem. 1997; 430: 227.
    • (1997) J. Electroanal. Chem. , vol.430 , pp. 227
    • Narvaez, A.1    Dominguez, E.2    Katakis, I.3    Katz, E.4    Ranjit, K.T.5    Ben-Dov, I.6    Willner, I.7
  • 14
    • 0026079376 scopus 로고
    • Use of 'solid-state' promoters in the electrochemistry of cytochrome c at a gold electrode
    • Santucci R, Faraoni A, Campanella L, Tranchida G, Brunori M. Use of 'solid-state' promoters in the electrochemistry of cytochrome c at a gold electrode. Biochem. J. 1991; 273: 783.
    • (1991) Biochem. J. , vol.273 , pp. 783
    • Santucci, R.1    Faraoni, A.2    Campanella, L.3    Tranchida, G.4    Brunori, M.5
  • 15
    • 0030722939 scopus 로고    scopus 로고
    • Microperoxidases catalytically degrade reactive oxygen species and may be anti-cataract agents
    • Spector A, Ma W, Wang RR, Kleiman NJ. Microperoxidases catalytically degrade reactive oxygen species and may be anti-cataract agents. Exp. Eye Res. 1997; 65: 457.
    • (1997) Exp. Eye Res. , vol.65 , pp. 457
    • Spector, A.1    Ma, W.2    Wang, R.R.3    Kleiman, N.J.4
  • 16
    • 0029090195 scopus 로고
    • The development of a peroxidase biosensor for monitoring phenol and related aromatic compounds
    • Ruzgas T, Emnéus J, Gorton L, Marko-Varga G. The development of a peroxidase biosensor for monitoring phenol and related aromatic compounds. Anal. Chim. Acta 1995; 311: 245.
    • (1995) Anal. Chim. Acta , vol.311 , pp. 245
    • Ruzgas, T.1    Emnéus, J.2    Gorton, L.3    Marko-Varga, G.4
  • 19
    • 0023255364 scopus 로고
    • Denitrification by a marine bacterium Pseudomonas nautica strain 617
    • Bonin P, Gilewicz M, Bertrand JC. Denitrification by a marine bacterium Pseudomonas nautica strain 617. Ann. Inst. Pasteur Microbiol., 1987; 138: 371.
    • (1987) Ann. Inst. Pasteur Microbiol. , vol.138 , pp. 371
    • Bonin, P.1    Gilewicz, M.2    Bertrand, J.C.3
  • 21
    • 0032981135 scopus 로고    scopus 로고
    • MAD structure of Pseudomonas nautica dimeric cytochrome c552 mimicks the c4 dihemic cytochrome domain association
    • Brown K, Nurizzo D, Besson S, Shepard W, Moura J, Moura I, Tegoni M, Cambillau C. MAD structure of Pseudomonas nautica dimeric cytochrome c552 mimicks the c4 dihemic cytochrome domain association. J. Mol. Biol. 1999; 289: 1017.
    • (1999) J. Mol. Biol. , vol.289 , pp. 1017
    • Brown, K.1    Nurizzo, D.2    Besson, S.3    Shepard, W.4    Moura, J.5    Moura, I.6    Tegoni, M.7    Cambillau, C.8
  • 25
    • 0041113733 scopus 로고
    • Mechanism of electrospray mass spectrometry. Electrospray as an electrolysis cell
    • Blades AT, Ikonomou MG, Kebarle P. Mechanism of electrospray mass spectrometry. Electrospray as an electrolysis cell. Anal. Chem. 1991; 63: 2109.
    • (1991) Anal. Chem. , vol.63 , pp. 2109
    • Blades, A.T.1    Ikonomou, M.G.2    Kebarle, P.3
  • 26
    • 0034582309 scopus 로고    scopus 로고
    • Unequivocal determination of metal atom oxidation state in naked heme proteins: Fe(III)myoglobin, Fe(III)cytochrome c, Fe(III)cytochrome b5, and Fe(III)cytochrome b5 L47R
    • He F, Hendrickson CL, Marshall AG. Unequivocal determination of metal atom oxidation state in naked heme proteins: Fe(III)myoglobin, Fe(III)cytochrome c, Fe(III)cytochrome b5, and Fe(III)cytochrome b5 L47R. J. Am. Soc. Mass Spectrom. 2000; 11: 12 0.
    • (2000) J. Am. Soc. Mass Spectrom. , vol.11 , pp. 120
    • He, F.1    Hendrickson, C.L.2    Marshall, A.G.3
  • 28
    • 0029645140 scopus 로고
    • Characterization of cytochrome c variants with high-resolution FT-ICR mass spectrometry-correlation of fragmentation and structure
    • Wu QY, van Orden S, Cheng XH, Bakhtiar R, Smith RD. Characterization of cytochrome c variants with high-resolution FT-ICR mass spectrometry-correlation of fragmentation and structure. Anal. Chem. 1995; 67: 2498.
    • (1995) Anal. Chem. , vol.67 , pp. 2498
    • Wu, Q.Y.1    Van Orden, S.2    Cheng, X.H.3    Bakhtiar, R.4    Smith, R.D.5
  • 29
    • 0000596572 scopus 로고
    • Studies on heme binding in myoglobin, hemoglobin, and cytochrome c by ion spray mass spectrometry
    • Li YT, Hsieh YL, Henion JD, Ganem B. Studies on heme binding in myoglobin, hemoglobin, and cytochrome c by ion spray mass spectrometry. J. Am. Soc. Mass Spectrom. 1993; 4: 631.
    • (1993) J. Am. Soc. Mass Spectrom. , vol.4 , pp. 631
    • Li, Y.T.1    Hsieh, Y.L.2    Henion, J.D.3    Ganem, B.4
  • 30
    • 0025861133 scopus 로고
    • Electrospray ionization of porphyrins using a quadrupole ion trap for mass analysis
    • VanBerkel GJ, McLuckey SA, Glish GL. Electrospray ionization of porphyrins using a quadrupole ion trap for mass analysis. Anal. Chem. 1991; 63: 1098.
    • (1991) Anal. Chem. , vol.63 , pp. 1098
    • VanBerkel, G.J.1    McLuckey, S.A.2    Glish, G.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.