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The binding site of cytochrome c peroxidase for cytochrome c has been extensively studied. For example: (a) Poulos, T. L.; Kraut, J. J. Biol. Chem. 1980, 255, 10322-10330. (b) Corin, A. F.; McLendon, G.; Zhang, Q.; Hake, R. A.; Falvo, J.; Lu, K. S.; Ciccarelli, R. B.; Holzschu, D. Biochemistry 1991, 30, 11585-11595. (c) Miller, M. A.; Liu, R.-Q.; Hahm, S.; Geren, L.; Hibdon, S.; Kraut, J.; Durham, B.; Millett, F. Biochemistry 1994, 33, 8686-8693. (d) Hake, R.; Corin, A.; McLendon, G. J. Am. Chem. Soc. 1997, 119, 10557-10558.
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The binding site of cytochrome c peroxidase for cytochrome c has been extensively studied. For example: (a) Poulos, T. L.; Kraut, J. J. Biol. Chem. 1980, 255, 10322-10330. (b) Corin, A. F.; McLendon, G.; Zhang, Q.; Hake, R. A.; Falvo, J.; Lu, K. S.; Ciccarelli, R. B.; Holzschu, D. Biochemistry 1991, 30, 11585-11595. (c) Miller, M. A.; Liu, R.-Q.; Hahm, S.; Geren, L.; Hibdon, S.; Kraut, J.; Durham, B.; Millett, F. Biochemistry 1994, 33, 8686-8693. (d) Hake, R.; Corin, A.; McLendon, G. J. Am. Chem. Soc. 1997, 119, 10557-10558.
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The binding site of cytochrome c peroxidase for cytochrome c has been extensively studied. For example: (a) Poulos, T. L.; Kraut, J. J. Biol. Chem. 1980, 255, 10322-10330. (b) Corin, A. F.; McLendon, G.; Zhang, Q.; Hake, R. A.; Falvo, J.; Lu, K. S.; Ciccarelli, R. B.; Holzschu, D. Biochemistry 1991, 30, 11585-11595. (c) Miller, M. A.; Liu, R.-Q.; Hahm, S.; Geren, L.; Hibdon, S.; Kraut, J.; Durham, B.; Millett, F. Biochemistry 1994, 33, 8686-8693. (d) Hake, R.; Corin, A.; McLendon, G. J. Am. Chem. Soc. 1997, 119, 10557-10558.
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The binding site of cytochrome c peroxidase for cytochrome c has been extensively studied. For example: (a) Poulos, T. L.; Kraut, J. J. Biol. Chem. 1980, 255, 10322-10330. (b) Corin, A. F.; McLendon, G.; Zhang, Q.; Hake, R. A.; Falvo, J.; Lu, K. S.; Ciccarelli, R. B.; Holzschu, D. Biochemistry 1991, 30, 11585-11595. (c) Miller, M. A.; Liu, R.-Q.; Hahm, S.; Geren, L.; Hibdon, S.; Kraut, J.; Durham, B.; Millett, F. Biochemistry 1994, 33, 8686-8693. (d) Hake, R.; Corin, A.; McLendon, G. J. Am. Chem. Soc. 1997, 119, 10557-10558.
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Recently, substrate binding sites of some peroxidases have been clarified by X-ray crystallography: (a) Itakura, H.; Oda, Y.; Fukuyama, K. FEBS Lett. 1997, 412, 107-110. (b) Henriksen, A.; Schuller, D. J.; Meno, K.; Welinder, K. G.; Smith, A. T.; Gajhede, M. Biochemistry 1998, 37, 8054-8060.
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Recently, substrate binding sites of some peroxidases have been clarified by X-ray crystallography: (a) Itakura, H.; Oda, Y.; Fukuyama, K. FEBS Lett. 1997, 412, 107-110. (b) Henriksen, A.; Schuller, D. J.; Meno, K.; Welinder, K. G.; Smith, A. T.; Gajhede, M. Biochemistry 1998, 37, 8054-8060.
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The introduction of an artificial binding site into cytochrome c peroxidase by use of site-directed mutagenesis has been recently reported by Goodin and his co-worker: Goodin, D. B.; Musah, R. A. Biochemistry 1997, 36, 11665-11674.
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Ryabov and co-workers have demonstrated the construction of an artificial binding site by chemical modification into horseradish peroxidase: Ryabov, A. D.; Goral, V. N.; Gorton, L.; Csöregi, E. Chem. Eur. J. 1999, 5, 961-967.
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0028209418
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Several groups have investigated the properties of binding sites in peroxidases by site-directed mutagenesis. For example: (a) Fitzgerald, M. M.; Churchill, M. J.; McRee, D. E.; Goodin, D. B. Biochemistry 1994, 33, 3807-3817. (b) Newmyer, S. L.; Oitiz de Montellano, P. R. J. Biol. Chem. 1995, 270, 19430-19438. (c) Savenkova, M. L; Newmyer, S. L.; Ortiz de Montellano, P. R. J. Biol. Chem. 1996, 271, 1996. (d) Rodriguez-Lopez, J. N.; Smith, A. T.; Thorneley, R. N. F. J. Biol. Chem. 1996, 277, 4023- 4030.
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Several groups have investigated the properties of binding sites in peroxidases by site-directed mutagenesis. For example: (a) Fitzgerald, M. M.; Churchill, M. J.; McRee, D. E.; Goodin, D. B. Biochemistry 1994, 33, 3807-3817. (b) Newmyer, S. L.; Oitiz de Montellano, P. R. J. Biol. Chem. 1995, 270, 19430-19438. (c) Savenkova, M. L; Newmyer, S. L.; Ortiz de Montellano, P. R. J. Biol. Chem. 1996, 271, 1996. (d) Rodriguez-Lopez, J. N.; Smith, A. T.; Thorneley, R. N. F. J. Biol. Chem. 1996, 277, 4023- 4030.
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0028209418
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Several groups have investigated the properties of binding sites in peroxidases by site-directed mutagenesis. For example: (a) Fitzgerald, M. M.; Churchill, M. J.; McRee, D. E.; Goodin, D. B. Biochemistry 1994, 33, 3807-3817. (b) Newmyer, S. L.; Oitiz de Montellano, P. R. J. Biol. Chem. 1995, 270, 19430-19438. (c) Savenkova, M. L; Newmyer, S. L.; Ortiz de Montellano, P. R. J. Biol. Chem. 1996, 271, 1996. (d) Rodriguez-Lopez, J. N.; Smith, A. T.; Thorneley, R. N. F. J. Biol. Chem. 1996, 277, 4023- 4030.
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Several groups have investigated the properties of binding sites in peroxidases by site-directed mutagenesis. For example: (a) Fitzgerald, M. M.; Churchill, M. J.; McRee, D. E.; Goodin, D. B. Biochemistry 1994, 33, 3807-3817. (b) Newmyer, S. L.; Oitiz de Montellano, P. R. J. Biol. Chem. 1995, 270, 19430-19438. (c) Savenkova, M. L; Newmyer, S. L.; Ortiz de Montellano, P. R. J. Biol. Chem. 1996, 271, 1996. (d) Rodriguez-Lopez, J. N.; Smith, A. T.; Thorneley, R. N. F. J. Biol. Chem. 1996, 277, 4023-4030.
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Thorneley, R.N.F.3
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0027509149
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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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Ortiz De Montellano, P.R.3
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0030001545
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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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Watanabe, Y.3
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24
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0029800365
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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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Nagano, S.2
Ishimori, K.3
Watanabe, Y.4
Morishima, I.5
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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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Ozaki, S.1
Matsui, T.2
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0031826090
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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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Mauk, A.G.6
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0028049452
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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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0344594229
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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.
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33
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0001279637
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(a) Tsukahara, K.; Okazawa, T.; Takahashi, H.; Yamamoto, Y. lnorg. Chem. 1986, 25, 4756-4760.
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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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39
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0344594228
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unpublished results
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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.
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Hayashi, T.1
Hitomi, Y.2
Hisaeda, Y.3
Ogoshi, H.4
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40
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0344162654
-
-
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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0004049513
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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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