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Volumn 120, Issue 20, 1998, Pages 4910-4915

Artificial protein-protein complexation between a reconstituted myoglobulin and cytochrome c

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; MYOGLOBIN; PORPHYRIN; PROTOPORPHYRIN;

EID: 0032572119     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9723951     Document Type: Article
Times cited : (56)

References (36)
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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.
    • (1997) Angew. Chem., Int. Ed. Engl. , vol.36 , pp. 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.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 542-543
    • Willner, I.1    Zahavy, E.2    Heleg-Shabtai, V.3
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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.
    • (1995) Chem. Lett. , pp. 911-912
    • Hayashi, T.1    Hitomi, Y.2    Suzuki, A.3    Takimura, T.4    Ogoshi, H.5
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    • In press
    • 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.
    • Inorg. Chim. Acta
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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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    • 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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    • 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.
  • 32
    • 0001102428 scopus 로고    scopus 로고
    • 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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    • Nocek, J.M.1    Zhou, J.S.2    Forest, S.D.3    Priyadarshy, S.4    Beratan, D.N.5    Onuchic, J.N.6    Hoffman, B.M.7
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    • Suslick, K. S., Ed.; Pergamon: Oxford
    • 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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    • references are cited therein
    • 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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