Substrates for rapid delivery of electrons and holes to buried active sites in proteins

Angewandte Chemie - International Edition

Volumn 38, Issue 1-2, 1999, Pages 89-92

  Wilker, Jonathan J ^a   Dmochowski, Ivan J ^a   Dawson, John H ^b   Winkler, Jay R ^a   Gray, Harry B ^a  

^a CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

^b UNIVERSITY OF SOUTH CAROLINA   (United States)

Author keywords

Electron transfer; Heme proteins; Metalloenzymes; Ruthenium; Sensitizers

Indexed keywords

ADAMANTANE; ENZYME; ETHYLBENZENE; HEMOPROTEIN; IMIDAZOLE; IRON; PHOTOSENSITIZING AGENT; PORPHYRIN; PROTEIN; RUTHENIUM;

ABSORPTION; ARTICLE; ELECTRON; ELECTRON TRANSPORT; PHOTOLYSIS;

EID: 0033555652     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1521-3773(19990115)38:1/2<89::aid-anie89>3.0.co;2-r     Document Type: Article

References (27)

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6. The synthesis of Ru-EB is typical: Reaction of thionyl chloride with 10-bromodecanoic acid, followed by addition of 4-ethylaniline, gives the corresponding amide. Addition of the amide to a solution of 4.4′-dimethyl-2.2′-bipyridine and lithium diisopropylamide yields the derivatized bpy, which was allowed to react with [RuCl2(bpy)2] to give Ru-EB.
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11. All studies were performed under an argon atmosphere with 10 μM ruthenium complex. 10 μM enzyme in 100 mM potassium chloride, and 20mM potassium phosphate buffer (pH 7.4) at room temperature.
12. T. L. Poulos, J. Cupp-Vickery, H. Li in ref. [2], pp. 125-150.
13. Excitation at 480 nm (20-ns pulse width); the experimental setup has been described.[5]
14. D = 0.68 μM.
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17. 0 values of derivatives with substrate-terminated hydrocarbon chains should be similar.
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19. I-EB displays a Soret peak at 390 nm.
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21. IV state of P450. Hydrogen bonding to this thiolate (T. L. Poulos, B. C. Finzel, A. J. Howard, J. Mol. Biol. 1987, 195, 687-700) , however, decreases the donor strength. Although the reaction product of iodosobenzene and P450 exhibits a Soret band at 393 nm (R. C. Blake H. M. J. Coon, J. Biol. Chem. 1989, 264, 3694-3701) , the Soret band of chloroperoxidase is red-shifted upon ferryl formation: R. Nakajima, I. Yamazaki, B. W. Griffi, Biochem. Biophys. Res. Commun. 1985, 128, 1-6) . The blue-shifted Soret band exhibited by the heme in the oxidized (Ru-EB)-P450 complex is not unlike that of P420, a common P450 decomposition product: S. A. Martinis, S. R. Blank, L. P. Hager, S. G. Sligar, G. H. B. Hoa, J. J. Rux, J. H. Dawson, Biochemistry 1996, 35, 14530-14536. Formation of P420, however, is largely irreversible, whereas oxidized (Ru-EB)-P450 returns to the resting state without appreciable decomposition.
22. IV state of P450. Hydrogen bonding to this thiolate (T. L. Poulos, B. C. Finzel, A. J. Howard, J. Mol. Biol. 1987, 195, 687-700) , however, decreases the donor strength. Although the reaction product of iodosobenzene and P450 exhibits a Soret band at 393 nm (R. C. Blake H. M. J. Coon, J. Biol. Chem. 1989, 264, 3694-3701) , the Soret band of chloroperoxidase is red-shifted upon ferryl formation: R. Nakajima, I. Yamazaki, B. W. Griffi, Biochem. Biophys. Res. Commun. 1985, 128, 1-6) . The blue-shifted Soret band exhibited by the heme in the oxidized (Ru-EB)-P450 complex is not unlike that of P420, a common P450 decomposition product: S. A. Martinis, S. R. Blank, L. P. Hager, S. G. Sligar, G. H. B. Hoa, J. J. Rux, J. H. Dawson, Biochemistry 1996, 35, 14530-14536. Formation of P420, however, is largely irreversible, whereas oxidized (Ru-EB)-P450 returns to the resting state without appreciable decomposition.
23. IV state of P450. Hydrogen bonding to this thiolate (T. L. Poulos, B. C. Finzel, A. J. Howard, J. Mol. Biol. 1987, 195, 687-700) , however, decreases the donor strength. Although the reaction product of iodosobenzene and P450 exhibits a Soret band at 393 nm (R. C. Blake H. M. J. Coon, J. Biol. Chem. 1989, 264, 3694-3701) , the Soret band of chloroperoxidase is red-shifted upon ferryl formation: R. Nakajima, I. Yamazaki, B. W. Griffi, Biochem. Biophys. Res. Commun. 1985, 128, 1-6) . The blue-shifted Soret band exhibited by the heme in the oxidized (Ru-EB)-P450 complex is not unlike that of P420, a common P450 decomposition product: S. A. Martinis, S. R. Blank, L. P. Hager, S. G. Sligar, G. H. B. Hoa, J. J. Rux, J. H. Dawson, Biochemistry 1996, 35, 14530-14536. Formation of P420, however, is largely irreversible, whereas oxidized (Ru-EB)-P450 returns to the resting state without appreciable decomposition.
24. IV state of P450. Hydrogen bonding to this thiolate (T. L. Poulos, B. C. Finzel, A. J. Howard, J. Mol. Biol. 1987, 195, 687-700) , however, decreases the donor strength. Although the reaction product of iodosobenzene and P450 exhibits a Soret band at 393 nm (R. C. Blake H. M. J. Coon, J. Biol. Chem. 1989, 264, 3694-3701) , the Soret band of chloroperoxidase is red-shifted upon ferryl formation: R. Nakajima, I. Yamazaki, B. W. Griffi, Biochem. Biophys. Res. Commun. 1985, 128, 1-6) . The blue-shifted Soret band exhibited by the heme in the oxidized (Ru-EB)-P450 complex is not unlike that of P420, a common P450 decomposition product: S. A. Martinis, S. R. Blank, L. P. Hager, S. G. Sligar, G. H. B. Hoa, J. J. Rux, J. H. Dawson, Biochemistry 1996, 35, 14530-14536. Formation of P420, however, is largely irreversible, whereas oxidized (Ru-EB)-P450 returns to the resting state without appreciable decomposition.
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