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Volumn 121, Issue 34, 1999, Pages 7747-7750

Peroxidase activity of myoglobin is enhanced by chemical mutation of heme-propionates

Author keywords

[No Author keywords available]

Indexed keywords

CATECHOL; FERROCYANIDE; GUAIACOL; HEME DERIVATIVE; HYDROGEN PEROXIDE; HYDROQUINONE; MYOGLOBIN; PEROXIDASE; PROPIONIC ACID;

EID: 0033199953     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9841005     Document Type: Article
Times cited : (96)

References (44)
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    • Furthermore, several groups have reported that some distal- or proximal-pocket mutants of myoglobin enhanced the peroxidase or peroxygenase activity. For example: (a) Rao, S. I.; Wilks, A.; Ortiz de Montellano, P. R. J. Biol. Chem. 1993, 268, 803-809. (b) Ozaki, S.; Matsui, T.; Watanabe, Y. J. Am. Chem. Soc. 1996, 118, 9784-9785. (c) Matsui, T.; Nagano, S.; Ishimori, K.; Watanabe, Y.; Morishima, I. Biochemistry 1996, 35, 13118-13124. (d) Ozaki, S.; Matsui, T.; Watanabe, Y. J. Am. Chem. Soc. 1997, 119, 6666-6667. (e) Hildebrand, D. P.; Lim, K.-T.; Rosell, F. I.; Twitchett, M. B.; Wan, L.; Mauk, A. G. J. Inorg. Biochem. 1998, 70, 11-16.
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    • Furthermore, several groups have reported that some distal- or proximal-pocket mutants of myoglobin enhanced the peroxidase or peroxygenase activity. For example: (a) Rao, S. I.; Wilks, A.; Ortiz de Montellano, P. R. J. Biol. Chem. 1993, 268, 803-809. (b) Ozaki, S.; Matsui, T.; Watanabe, Y. J. Am. Chem. Soc. 1996, 118, 9784-9785. (c) Matsui, T.; Nagano, S.; Ishimori, K.; Watanabe, Y.; Morishima, I. Biochemistry 1996, 35, 13118-13124. (d) Ozaki, S.; Matsui, T.; Watanabe, Y. J. Am. Chem. Soc. 1997, 119, 6666-6667. (e) Hildebrand, D. P.; Lim, K.-T.; Rosell, F. I.; Twitchett, M. B.; Wan, L.; Mauk, A. G. J. Inorg. Biochem. 1998, 70, 11-16.
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    • Furthermore, several groups have reported that some distal- or proximal-pocket mutants of myoglobin enhanced the peroxidase or peroxygenase activity. For example: (a) Rao, S. I.; Wilks, A.; Ortiz de Montellano, P. R. J. Biol. Chem. 1993, 268, 803-809. (b) Ozaki, S.; Matsui, T.; Watanabe, Y. J. Am. Chem. Soc. 1996, 118, 9784-9785. (c) Matsui, T.; Nagano, S.; Ishimori, K.; Watanabe, Y.; Morishima, I. Biochemistry 1996, 35, 13118-13124. (d) Ozaki, S.; Matsui, T.; Watanabe, Y. J. Am. Chem. Soc. 1997, 119, 6666-6667. (e) Hildebrand, D. P.; Lim, K.-T.; Rosell, F. I.; Twitchett, M. B.; Wan, L.; Mauk, A. G. J. Inorg. Biochem. 1998, 70, 11-16.
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    • Furthermore, several groups have reported that some distal- or proximal-pocket mutants of myoglobin enhanced the peroxidase or peroxygenase activity. For example: (a) Rao, S. I.; Wilks, A.; Ortiz de Montellano, P. R. J. Biol. Chem. 1993, 268, 803-809. (b) Ozaki, S.; Matsui, T.; Watanabe, Y. J. Am. Chem. Soc. 1996, 118, 9784-9785. (c) Matsui, T.; Nagano, S.; Ishimori, K.; Watanabe, Y.; Morishima, I. Biochemistry 1996, 35, 13118-13124. (d) Ozaki, S.; Matsui, T.; Watanabe, Y. J. Am. Chem. Soc. 1997, 119, 6666-6667. (e) Hildebrand, D. P.; Lim, K.-T.; Rosell, F. I.; Twitchett, M. B.; Wan, L.; Mauk, A. G. J. Inorg. Biochem. 1998, 70, 11-16.
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    • Furthermore, several groups have reported that some distal- or proximal-pocket mutants of myoglobin enhanced the peroxidase or peroxygenase activity. For example: (a) Rao, S. I.; Wilks, A.; Ortiz de Montellano, P. R. J. Biol. Chem. 1993, 268, 803-809. (b) Ozaki, S.; Matsui, T.; Watanabe, Y. J. Am. Chem. Soc. 1996, 118, 9784-9785. (c) Matsui, T.; Nagano, S.; Ishimori, K.; Watanabe, Y.; Morishima, I. Biochemistry 1996, 35, 13118-13124. (d) Ozaki, S.; Matsui, T.; Watanabe, Y. J. Am. Chem. Soc. 1997, 119, 6666-6667. (e) Hildebrand, D. P.; Lim, K.-T.; Rosell, F. I.; Twitchett, M. B.; Wan, L.; Mauk, A. G. J. Inorg. Biochem. 1998, 70, 11-16.
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    • 1H NMR spectrum of deoxy rMb(1) reduced by dithionite also shows the typical deoxy high spin state of horse heart Mb. The spectrum is shown in Supporting Information. Busse, S. C.; Jue. T. Biochemistry 1994, 33, 10934-10943.
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    • The CD spectrum of rMb(1) is also comparable with that of nMb
    • The CD spectrum of rMb(1) is also comparable with that of nMb.
  • 38
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    • Abbreviations: rMb(1)-II and nMb-II represent compound II-like oxoferryl species of rMb(1) and nMb, respectively
    • Abbreviations: rMb(1)-II and nMb-II represent compound II-like oxoferryl species of rMb(1) and nMb, respectively.
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    • unpublished results
    • Catalytic oxidation of ferrocytochrome c is also accelerated by rMb-(1) in the presence of hydrogen peroxide. Hayashi, T.; Hitomi, Y.; Hisaeda, Y.; Ogoshi, H., unpublished results.
    • Hayashi, T.1    Hitomi, Y.2    Hisaeda, Y.3    Ogoshi, H.4
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    • Oxidation rate of ferrocyanide by rMb(1) depends on the ionic strength of buffer solution. The oxidation activity dramatically decreases to 2% of that observed for nMb at 10 mM ionic strength
    • Oxidation rate of ferrocyanide by rMb(1) depends on the ionic strength of buffer solution. The oxidation activity dramatically decreases to 2% of that observed for nMb at 10 mM ionic strength.
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    • i = 19 ± 1 mM: (a) Enzyme Assays; Eisenthal, R., Danson, M. J., Eds.; Oxford University Press: Oxford, 1992. (b) Song, Y.; Yang, C.-M.; Kluger, R. J. Am. Chem. Soc. 1993, 115, 4365-4366.
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