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For recent examples of artificial assembly system of hemoprotein, cf.: (a) Zhou, J. S.; Granada, E. S. V.; Leontis, N. B.; Rodgers, M. A. J. J. Am. Chem. Soc. 1990, 112, 5074-5080. (b) Lahiri, J.; Fate, G. D.; Ungashe, S. B.; Groves, J. T. J. Am. Chem. Soc. 1996, 118, 2347-2358. (c) Tsukahara, K.; Kimura, C. J. Electroanal. Chem. 1997, 438, 67-70. (d) Hamuro, Y.; Calama, M. C.; Park, H. S.; Hamilton, A. D. Angew. Chem., Int. Ed. Engl. 1997, 36, 2680-2683.
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For recent examples of artificial assembly system of hemoprotein, cf.: (a) Zhou, J. S.; Granada, E. S. V.; Leontis, N. B.; Rodgers, M. A. J. J. Am. Chem. Soc. 1990, 112, 5074-5080. (b) Lahiri, J.; Fate, G. D.; Ungashe, S. B.; Groves, J. T. J. Am. Chem. Soc. 1996, 118, 2347-2358. (c) Tsukahara, K.; Kimura, C. J. Electroanal. Chem. 1997, 438, 67-70. (d) Hamuro, Y.; Calama, M. C.; Park, H. S.; Hamilton, A. D. Angew. Chem., Int. Ed. Engl. 1997, 36, 2680-2683.
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For recent examples of artificial assembly system of hemoprotein, cf.: (a) Zhou, J. S.; Granada, E. S. V.; Leontis, N. B.; Rodgers, M. A. J. J. Am. Chem. Soc. 1990, 112, 5074-5080. (b) Lahiri, J.; Fate, G. D.; Ungashe, S. B.; Groves, J. T. J. Am. Chem. Soc. 1996, 118, 2347-2358. (c) Tsukahara, K.; Kimura, C. J. Electroanal. Chem. 1997, 438, 67-70. (d) Hamuro, Y.; Calama, M. C.; Park, H. S.; Hamilton, A. D. Angew. Chem., Int. Ed. Engl. 1997, 36, 2680-2683.
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For examples of reconstituted myoglobin, cf.: (a) Suzuki, A.; Okuda, K.; Kawagoe, K.; Toi, H.; Aoyama, Y.; Ogoshi, H. Chem. Lett. 1985, 1169-1172. (b) Hamachi, I.; Tajiri, Y.; Shinkai, S. J. Am. Chem. Soc. 1994, 116, 7437-7438. (c) Willner, I.; Zahavy, E.; Heleg-Shabtai, V. J. Am. Chem. Soc. 1995, 117, 542-543. (d) Hayashi, T.; Hitomi, Y.; Suzuki, A.; Takimura, T.; Ogoshi, H. Chem. Lett. 1995, 911-912. (e) Hayashi, T.; Takimura, T.; Aoyama, Y.; Hitomi, Y.; Suzuki, A.; Ogoshi, H. Inorg. Chim. Acta In press.
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For examples of reconstituted myoglobin, cf.: (a) Suzuki, A.; Okuda, K.; Kawagoe, K.; Toi, H.; Aoyama, Y.; Ogoshi, H. Chem. Lett. 1985, 1169-1172. (b) Hamachi, I.; Tajiri, Y.; Shinkai, S. J. Am. Chem. Soc. 1994, 116, 7437-7438. (c) Willner, I.; Zahavy, E.; Heleg-Shabtai, V. J. Am. Chem. Soc. 1995, 117, 542-543. (d) Hayashi, T.; Hitomi, Y.; Suzuki, A.; Takimura, T.; Ogoshi, H. Chem. Lett. 1995, 911-912. (e) Hayashi, T.; Takimura, T.; Aoyama, Y.; Hitomi, Y.; Suzuki, A.; Ogoshi, H. Inorg. Chim. Acta In press.
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For examples of reconstituted myoglobin, cf.: (a) Suzuki, A.; Okuda, K.; Kawagoe, K.; Toi, H.; Aoyama, Y.; Ogoshi, H. Chem. Lett. 1985, 1169-1172. (b) Hamachi, I.; Tajiri, Y.; Shinkai, S. J. Am. Chem. Soc. 1994, 116, 7437-7438. (c) Willner, I.; Zahavy, E.; Heleg-Shabtai, V. J. Am. Chem. Soc. 1995, 117, 542-543. (d) Hayashi, T.; Hitomi, Y.; Suzuki, A.; Takimura, T.; Ogoshi, H. Chem. Lett. 1995, 911-912. (e) Hayashi, T.; Takimura, T.; Aoyama, Y.; Hitomi, Y.; Suzuki, A.; Ogoshi, H. Inorg. Chim. Acta In press.
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For examples of reconstituted myoglobin, cf.: (a) Suzuki, A.; Okuda, K.; Kawagoe, K.; Toi, H.; Aoyama, Y.; Ogoshi, H. Chem. Lett. 1985, 1169-1172. (b) Hamachi, I.; Tajiri, Y.; Shinkai, S. J. Am. Chem. Soc. 1994, 116, 7437-7438. (c) Willner, I.; Zahavy, E.; Heleg-Shabtai, V. J. Am. Chem. Soc. 1995, 117, 542-543. (d) Hayashi, T.; Hitomi, Y.; Suzuki, A.; Takimura, T.; Ogoshi, H. Chem. Lett. 1995, 911-912. (e) Hayashi, T.; Takimura, T.; Aoyama, Y.; Hitomi, Y.; Suzuki, A.; Ogoshi, H. Inorg. Chim. Acta In press.
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For examples of reconstituted myoglobin, cf.: (a) Suzuki, A.; Okuda, K.; Kawagoe, K.; Toi, H.; Aoyama, Y.; Ogoshi, H. Chem. Lett. 1985, 1169-1172. (b) Hamachi, I.; Tajiri, Y.; Shinkai, S. J. Am. Chem. Soc. 1994, 116, 7437-7438. (c) Willner, I.; Zahavy, E.; Heleg-Shabtai, V. J. Am. Chem. Soc. 1995, 117, 542-543. (d) Hayashi, T.; Hitomi, Y.; Suzuki, A.; Takimura, T.; Ogoshi, H. Chem. Lett. 1995, 911-912. (e) Hayashi, T.; Takimura, T.; Aoyama, Y.; Hitomi, Y.; Suzuki, A.; Ogoshi, H. Inorg. Chim. Acta In press.
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3* → ferricytochrome c is estimated to be ca. 1.1 eV by use of the following papers: Armstrong, F. A.; Hill, H. A. O.; Walton, N. J. Q. Rev. Biophys. 1986, 18, 261-322. Cheng, J.; Zhou, J. S.; Kostić, N. M. Inorg. Chem. 1994, 33, 1600-1606.
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0001168330
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3* → ferricytochrome c is estimated to be ca. 1.1 eV by use of the following papers: Armstrong, F. A.; Hill, H. A. O.; Walton, N. J. Q. Rev. Biophys. 1986, 18, 261-322. Cheng, J.; Zhou, J. S.; Kostić, N. M. Inorg. Chem. 1994, 33, 1600-1606.
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5. In this system, a single-exponential decay was observed due to the fast dissociation of the complex. Our system could be followed by the same kinetic model as their case. Nocek, J. M.; Sishta, B. P.; Cameron, J. C.; Mauk, A. G.; Hoffman, B. M. J. Am. Chem. Soc. 1997, 119, 2146-2155.
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31
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2642653397
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-
note
-
Figure 6 also reveals that the binding affinity remarkably decreases at higher ionic strength, although it is difficult to obtain accurate parameters at higher ionic strength due to the insufficient curvature of the plots.
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32
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0001102428
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For recent reviews, see: (a) Nocek, J. M.; Zhou, J. S.; Forest, S. D.; Priyadarshy, S.; Beratan, D. N.; Onuchic, J. N.; Hoffman, B. M. Chem. Rev. 1996, 96, 2459-2489. (b) Durham, B.; Millett, F. S. In Comprehensive Supramolecular Chemistry; Suslick, K. S., Ed.; Pergamon: Oxford, 1996; Vol. 5, pp 219-247. (c) McLendon, G.; Hake, R. Chem. Rev. 1992, 92, 481-490. references are cited therein.
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Hoffman, B.M.7
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Suslick, K. S., Ed.; Pergamon: Oxford
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For recent reviews, see: (a) Nocek, J. M.; Zhou, J. S.; Forest, S. D.; Priyadarshy, S.; Beratan, D. N.; Onuchic, J. N.; Hoffman, B. M. Chem. Rev. 1996, 96, 2459-2489. (b) Durham, B.; Millett, F. S. In Comprehensive Supramolecular Chemistry; Suslick, K. S., Ed.; Pergamon: Oxford, 1996; Vol. 5, pp 219-247. (c) McLendon, G.; Hake, R. Chem. Rev. 1992, 92, 481-490. references are cited therein.
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For recent reviews, see: (a) Nocek, J. M.; Zhou, J. S.; Forest, S. D.; Priyadarshy, S.; Beratan, D. N.; Onuchic, J. N.; Hoffman, B. M. Chem. Rev. 1996, 96, 2459-2489. (b) Durham, B.; Millett, F. S. In Comprehensive Supramolecular Chemistry; Suslick, K. S., Ed.; Pergamon: Oxford, 1996; Vol. 5, pp 219-247. (c) McLendon, G.; Hake, R. Chem. Rev. 1992, 92, 481-490. references are cited therein.
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