메뉴 건너뛰기




Volumn 4, Issue 3, 1997, Pages 215-221

Construction and characterization of a manganese-binding site in cytochrome c peroxidase: Towards a novel manganese peroxidase

Author keywords

bioinorganic chemistry; metalloprotein; paramagnetic NMR; protein engineering; site directed mutagenesis

Indexed keywords

ARACHIS HYPOGAEA;

EID: 0031104643     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(97)90291-X     Document Type: Article
Times cited : (62)

References (38)
  • 1
    • 0029016430 scopus 로고
    • Protein design: Novel metal binding sites
    • Regan, L. (1995). Protein design: novel metal binding sites. Trends Biochem. Sci. 20, 280-285.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 280-285
    • Regan, L.1
  • 2
    • 14744283294 scopus 로고
    • Protein stabilization by engineered metal chelation
    • Kellis, J.T., Jr, Todd, R.J. & Arnold, F.H. (1991). Protein stabilization by engineered metal chelation. Biotechnology 9, 994-995.
    • (1991) Biotechnology , vol.9 , pp. 994-995
    • Kellis Jr., J.T.1    Todd, R.J.2    Arnold, F.H.3
  • 3
    • 0024864423 scopus 로고
    • Extracellular peroxidases involved in lignin degradation by the white rot basidiomycete Phanerochaete chrysosporium
    • (Whitaker, J.R. & Sonnet, P.E., eds), American Chemical Society, Washington, DC, USA
    • Gold, M.H., Wariishi, H. & Valli, K. (1989). Extracellular peroxidases involved in lignin degradation by the white rot basidiomycete Phanerochaete chrysosporium. In Biocatalysis in Agricultural Biotechnology. (Whitaker, J.R. & Sonnet, P.E., eds), pp. 127-140, American Chemical Society, Washington, DC, USA.
    • (1989) Biocatalysis in Agricultural Biotechnology , pp. 127-140
    • Gold, M.H.1    Wariishi, H.2    Valli, K.3
  • 4
    • 0027180067 scopus 로고
    • Molecular biology of the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • Gold, M. & Alic, M. (1993). Molecular biology of the lignin-degrading basidiomycete Phanerochaete chrysosporium. Microbiol. Rev. 57, 605-622.
    • (1993) Microbiol. Rev. , vol.57 , pp. 605-622
    • Gold, M.1    Alic, M.2
  • 5
    • 84982512382 scopus 로고
    • Biodegradation of environmental pollutants by the white rot fungus Phanerochaete chrysosporium: Involvement of the lignin degrading system
    • Bumpus, J.A. & Aust, S.D. (1987). Biodegradation of environmental pollutants by the white rot fungus Phanerochaete chrysosporium: involvement of the lignin degrading system. Bioessays 6, 166-170.
    • (1987) Bioessays , vol.6 , pp. 166-170
    • Bumpus, J.A.1    Aust, S.D.2
  • 6
    • 0022060044 scopus 로고
    • Mineralization of polychlorinated biphenyls by Phanerochaete chrysosporium: A ligninolytic fungus
    • Eaton, D.C. (1985). Mineralization of polychlorinated biphenyls by Phanerochaete chrysosporium: a ligninolytic fungus. Enzyme Microb. Technol. 7, 194-196.
    • (1985) Enzyme Microb. Technol. , vol.7 , pp. 194-196
    • Eaton, D.C.1
  • 7
    • 0028888065 scopus 로고
    • Potential for bioremediation of xenobiotic compounds by the white-rot fungus Phanerochaete chrysosporium
    • Paszczynski, A. & Crawford, R.L. (1995). Potential for bioremediation of xenobiotic compounds by the white-rot fungus Phanerochaete chrysosporium. Biotechnol. Prog. 11, 368-379.
    • (1995) Biotechnol. Prog. , vol.11 , pp. 368-379
    • Paszczynski, A.1    Crawford, R.L.2
  • 8
    • 0028587337 scopus 로고
    • The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06 Å resolution
    • Sundaramoorthy, M., Kishi, K., Gold, M.H. & Poulos, T.L. (1994). The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06 Å resolution. J. Biol. Chem. 269, 32759-32767.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32759-32767
    • Sundaramoorthy, M.1    Kishi, K.2    Gold, M.H.3    Poulos, T.L.4
  • 9
    • 0027249006 scopus 로고
    • Kinetic analysis of manganese peroxidase
    • Kuan, I.-C., Johnson, K.A. & Tien, M. (1993). Kinetic analysis of manganese peroxidase. J. Biol. Chem. 268, 20064-20070.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20064-20070
    • Kuan, I.-C.1    Johnson, K.A.2    Tien, M.3
  • 10
    • 0030036165 scopus 로고    scopus 로고
    • Characterization of manganese(II) binding site mutants of manganese peroxidase
    • Kishi, K., Someren, M.K., Mayfield, M.B., Sun, J., Loehr, T.M. & Gold, M.H. (1996). Characterization of manganese(II) binding site mutants of manganese peroxidase. Biochemistry 35, 8986-8994.
    • (1996) Biochemistry , vol.35 , pp. 8986-8994
    • Kishi, K.1    Someren, M.K.2    Mayfield, M.B.3    Sun, J.4    Loehr, T.M.5    Gold, M.H.6
  • 11
    • 0027096634 scopus 로고
    • Manganese(II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium
    • Wariishi, H., Valli, K. & Gold, M.H. (1992). Manganese(II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. J. Biol. Chem. 267, 23688-23695.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23688-23695
    • Wariishi, H.1    Valli, K.2    Gold, M.H.3
  • 12
    • 0029646104 scopus 로고
    • The crystal structure of chloroperoxidase: A heme peroxidase-cytochrome P450 functional hybrid
    • Sundaramoorthy, M., Terner, J. & Poulos, T.L. (1995). The crystal structure of chloroperoxidase: a heme peroxidase-cytochrome P450 functional hybrid. Structure 3, 1367-1377.
    • (1995) Structure , vol.3 , pp. 1367-1377
    • Sundaramoorthy, M.1    Terner, J.2    Poulos, T.L.3
  • 13
    • 0028543703 scopus 로고
    • Evidence for the presence of Mn(II) in a peanut peroxidase. An EPR Study
    • Rodriguez Marañón, M.J., Hoy, A.R. & Van Huystee, R.B. (1994). Evidence for the presence of Mn(II) in a peanut peroxidase. An EPR study. Cell. Mol. Biol. 40, 871-879.
    • (1994) Cell. Mol. Biol. , vol.40 , pp. 871-879
    • Rodriguez Marañón, M.J.1    Hoy, A.R.2    Van Huystee, R.B.3
  • 14
    • 0000170196 scopus 로고
    • Yeast cytochrome c peroxidase
    • (Everse, J. & Grisham, M.B., eds) CRC Press: Boca Raton, FL, USA
    • Bosshard, H.R., Anni, H. & Yonetani, T. (1991). Yeast cytochrome c peroxidase. In Peroxidases in Chemistry and Biology, II. (Everse, J. & Grisham, M.B., eds) pp. 51-84, CRC Press: Boca Raton, FL, USA.
    • (1991) Peroxidases in Chemistry and Biology , vol.2 , pp. 51-84
    • Bosshard, H.R.1    Anni, H.2    Yonetani, T.3
  • 15
    • 0021723457 scopus 로고
    • Crystal structure of yeast cytochrome c peroxidase refined at 1.7 Å resolution
    • Finzel, B.C., Poulos, T.L. & Kraut, J. (1984). Crystal structure of yeast cytochrome c peroxidase refined at 1.7 Å resolution. J. Biol. Chem. 259, 13027-13036.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13027-13036
    • Finzel, B.C.1    Poulos, T.L.2    Kraut, J.3
  • 16
    • 0023106193 scopus 로고
    • Yeast cytochrome c peroxidase: Mutagenesis and expression in Escherichia colui show trptophan-51 is not the radical site in compound I
    • Fishel, L.A., Villafranca, J.E., Mauro, J.M. & Kraut, J. (1987). Yeast cytochrome c peroxidase: mutagenesis and expression in Escherichia colui show trptophan-51 is not the radical site in compound I. Biochemistry 26, 351-360.
    • (1987) Biochemistry , vol.26 , pp. 351-360
    • Fishel, L.A.1    Villafranca, J.E.2    Mauro, J.M.3    Kraut, J.4
  • 17
    • 0028137199 scopus 로고
    • Role of the proximal ligand in peroxidase catalysis
    • Choudhury, K., et al., & Poulos, T.L. (1994). Role of the proximal ligand in peroxidase catalysis. J. Biol. Chem. 269, 20239-20249.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20239-20249
    • Choudhury, K.1    Poulos, T.L.2
  • 18
    • 0025863971 scopus 로고
    • Amino acid substitutions at tryptophan-51 of cytochrome c peroxidase: Effects on coordination, species preference for cytochrome c, and electron transfer
    • Goodin, D.B., Davison, M.G., Roe, J.A., Mauk, A.G. & Smith, M. (1991). Amino acid substitutions at tryptophan-51 of cytochrome c peroxidase: effects on coordination, species preference for cytochrome c, and electron transfer. Biochemistry 30, 4953-4962.
    • (1991) Biochemistry , vol.30 , pp. 4953-4962
    • Goodin, D.B.1    Davison, M.G.2    Roe, J.A.3    Mauk, A.G.4    Smith, M.5
  • 20
    • 0023000125 scopus 로고
    • Resonance Raman study on cytochrome c peroxidase and its intermediate. Presence of the Fe(IV) = O bond in compound ES and heme-linked ionization
    • Hashimoto, S., Teraoka, J., Inubushi, T., Yonetani, T. & Kitagawa, T. (1986). Resonance Raman study on cytochrome c peroxidase and its intermediate. Presence of the Fe(IV) = O bond in compound ES and heme-linked ionization. J. Biol. Chem. 261, 11110-11118.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11110-11118
    • Hashimoto, S.1    Teraoka, J.2    Inubushi, T.3    Yonetani, T.4    Kitagawa, T.5
  • 21
    • 0024296692 scopus 로고
    • Spectral characterization of manganese peroxidase, an extracellular heme enzyme from the lignin-degrading basidiomycete, Phanerochaete chrysosporium
    • Mino, Y., Wariishi, H., Blackburn, N.J., Loehr, T.M. & Gold, M.H. (1988). Spectral characterization of manganese peroxidase, an extracellular heme enzyme from the lignin-degrading basidiomycete, Phanerochaete chrysosporium. J. Biol. Chem. 263, 7029-7036.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7029-7036
    • Mino, Y.1    Wariishi, H.2    Blackburn, N.J.3    Loehr, T.M.4    Gold, M.H.5
  • 22
    • 0001215890 scopus 로고
    • Nuclear magnetic resonance of paramagnetic metalloproteins
    • Bertini, I., Turano, P. & Vila, A.J. (1993). Nuclear magnetic resonance of paramagnetic metalloproteins. Chem. Rev. 93, 2833-2892.
    • (1993) Chem. Rev. , vol.93 , pp. 2833-2892
    • Bertini, I.1    Turano, P.2    Vila, A.J.3
  • 23
    • 0029310668 scopus 로고
    • pH-Dependent equilibria of yeast Met80Ala-iso-1 -cytochrome c probed by NMR spectroscopy: A comparison with the wild-type protein
    • Banci, L., Bertini, I., Bren, K.L., Gray, H.B. & Turano, P. (1995). pH-Dependent equilibria of yeast Met80Ala-iso-1 -cytochrome c probed by NMR spectroscopy: a comparison with the wild-type protein. Chem. Biol. 2, 377-383.
    • (1995) Chem. Biol. , vol.2 , pp. 377-383
    • Banci, L.1    Bertini, I.2    Bren, K.L.3    Gray, H.B.4    Turano, P.5
  • 24
    • 0027158797 scopus 로고
    • Binding of horseradish, lignin, and manganese peroxidase to their respective substrates
    • Banci, L., Bertini, I., Bini, T., Tien, M. & Turano, P. (1993). Binding of horseradish, lignin, and manganese peroxidase to their respective substrates. Biochemistry 32, 5825-5831.
    • (1993) Biochemistry , vol.32 , pp. 5825-5831
    • Banci, L.1    Bertini, I.2    Bini, T.3    Tien, M.4    Turano, P.5
  • 25
    • 0028169593 scopus 로고
    • The effect of the Asn82→Asp mutation in yeast cytochrome c peroxidase studied by proton NMR spectroscopy
    • Satterlee, J.D., Alam, S.L., Mauro, M.J., Erman, J.E. & Poulos, T.L. (1994). The effect of the Asn82→Asp mutation in yeast cytochrome c peroxidase studied by proton NMR spectroscopy. Eur. J. Biochem. 224, 81-87.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 81-87
    • Satterlee, J.D.1    Alam, S.L.2    Mauro, M.J.3    Erman, J.E.4    Poulos, T.L.5
  • 27
    • 0001956446 scopus 로고
    • NMR Methodology for Paramagnetic Proteins
    • (Berliner, L.J. & Reuben, J., eds), Plenum Press, NY, USA
    • La Mar, G.N. & De Ropp, J.S. (1993). NMR Methodology for Paramagnetic Proteins. In Biological Magnetic Resonance. (Berliner, L.J. & Reuben, J., eds), pp. 1-78, Plenum Press, NY, USA.
    • (1993) Biological Magnetic Resonance , pp. 1-78
    • La Mar, G.N.1    De Ropp, J.S.2
  • 28
    • 0025079270 scopus 로고
    • Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp→Asn235 mutant
    • Satterlee, J.D., Erman, J.E., Mauro, M.J. & Kraut, J. (1990). Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp→Asn235 mutant. Biochemistry 29, 8797-8804.
    • (1990) Biochemistry , vol.29 , pp. 8797-8804
    • Satterlee, J.D.1    Erman, J.E.2    Mauro, M.J.3    Kraut, J.4
  • 29
    • 0027421337 scopus 로고
    • Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I
    • Erman, J.E., Vitello, L.B., Miller, M.A., Shaw, A., Brown, K.A. & Kraut, J. (1993). Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I. Biochemistry 32, 9798-9806.
    • (1993) Biochemistry , vol.32 , pp. 9798-9806
    • Erman, J.E.1    Vitello, L.B.2    Miller, M.A.3    Shaw, A.4    Brown, K.A.5    Kraut, J.6
  • 30
    • 0028139313 scopus 로고
    • Homologous expression of recombinant manganese peroxidase in Phanerochaete chrysosporium
    • Mayfield, M.B., Kishi, K., Alic, M. & Gold, M.H. (1994). Homologous expression of recombinant manganese peroxidase in Phanerochaete chrysosporium. Appl. Environ. Microbiol. 60, 4303-4309.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 4303-4309
    • Mayfield, M.B.1    Kishi, K.2    Alic, M.3    Gold, M.H.4
  • 31
    • 0000462317 scopus 로고    scopus 로고
    • Direct measurement of the reduction potential of catalytically active cytochrome c peroxidase compound I: Voltammetric detection of a reversible, cooperative two-electron transfer reaction
    • Mondai, M.S., Fuller, H.A. & Armstrong, F.A. (1996). Direct measurement of the reduction potential of catalytically active cytochrome c peroxidase compound I: voltammetric detection of a reversible, cooperative two-electron transfer reaction. J. Am. Chem. Soc, 118, 263-264.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 263-264
    • Mondai, M.S.1    Fuller, H.A.2    Armstrong, F.A.3
  • 32
    • 0024473758 scopus 로고
    • Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES
    • Sivaraja, M., Goodin, D.B., Smith, M. & Hoffman, B.M. (1989). Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES. Science 245, 738-740.
    • (1989) Science , vol.245 , pp. 738-740
    • Sivaraja, M.1    Goodin, D.B.2    Smith, M.3    Hoffman, B.M.4
  • 33
    • 0015416039 scopus 로고
    • Enthalpy of decomposition of hydrogen peroxide by catalase at 25°C
    • Nelson, D.P. & Kiesow, L.A. (1972). Enthalpy of decomposition of hydrogen peroxide by catalase at 25°C. Anal. Biochem. 49, 474-478.
    • (1972) Anal. Biochem. , vol.49 , pp. 474-478
    • Nelson, D.P.1    Kiesow, L.A.2
  • 35
    • 0026972793 scopus 로고
    • Polymerase chain reaction (PCR) techniques for site-directed mutagenesis
    • Reikofski, J. & Tao, B.Y. (1992). Polymerase chain reaction (PCR) techniques for site-directed mutagenesis. Biotech. Adv. 10, 535-547.
    • (1992) Biotech. Adv. , vol.10 , pp. 535-547
    • Reikofski, J.1    Tao, B.Y.2
  • 37
    • 0006739227 scopus 로고
    • A spectrophotometric method for the simultaneous determination of myoglobin and hemoglobin in extracts of human muscle
    • De Duve, C. (1948). A spectrophotometric method for the simultaneous determination of myoglobin and hemoglobin in extracts of human muscle. Acta Chem. Scand. 2, 264-289.
    • (1948) Acta Chem. Scand. , vol.2 , pp. 264-289
    • De Duve, C.1
  • 38
    • 0013790866 scopus 로고
    • Determination of heme a concentration in cytochrome preparations by hemochromogen method
    • Morrison, M. & Horie, S. (1965). Determination of heme a concentration in cytochrome preparations by hemochromogen method. Anal. Biochem. 12, 77-82.
    • (1965) Anal. Biochem. , vol.12 , pp. 77-82
    • Morrison, M.1    Horie, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.