Molecular orientation distributions in protein films. 2. Site-directed immobilization of yeast cytochrome c on thiol-capped, self-assembled monolayers

Journal of the American Chemical Society

Volumn 119, Issue 3, 1997, Pages 571-576

  Edmiston, Paul L ^a   Lee, John E ^a   Cheng, Shin Song ^a   Saavedra, S Scott ^a  

^a University of Arizona ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C;

ARTICLE; ENZYME IMMOBILIZATION; ENZYME STRUCTURE; MOLECULAR DYNAMICS; SURFACE PROPERTY; THERMODYNAMICS;

EID: 1842327453     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9623673     Document Type: Article

References (62)

1. (a) Brash, J. L.; Horbett, T. A. In Proteins at Interfaces II, Horbett, T. A., Brash, J. L., Eds.; ACS Symposium Series 602; American Chemical Society: Washingotn, DC, 1995; pp 1-23 and references therein,
2. (b) Hlady, V.; Buijs, J. Curr. Opin. Biotechnol. 1996, 7, 72-77 and references therein.
3. (a) Andrade, J. D.; Hlady, V. Adv. Polym. Sci. 1986, 79, 1-63.
4. (b) Haynes, C. A.; Norde, W. Colloids Surf. B: Biointerfaces 1994, 2, 517-566.
5. Swalen, J. D.; Allara, D. L.; Andrade, J. D.; Chandross, E. A.; Garoff, S.; Israelchvili, J.; McCarthy, T. J.; Murray, R.; Pease, R. F.; Rabolt, J. F.; Wynne, K. J.; Yu, H. Langmuir 1987, 3, 932-950.
6. Lee, J. E; Saavedra, S. S. Langmuir 1996, 12, 4025-4032.
7. (a) Tarlov, M. J.; Bowden, E. F. J. Am. Chem. Soc. 1991, 113, 1847-1849.
8. (b) Cullison, J. K.; Hawkridge, F. M.; Nakashima, N.; Yoshikawa, S. Langmuir 1994, 10, 877-882.
9. (a) Chang, I.-N.; Herron, J. N. Langmuir 1995, 11, 2083-2089.
10. (b) Lin, J.-N.; Chang, I.-N.; Andrade, J. D.; Herron, J. N.; Christensen, D. A. 1991 J. Chromatogr. 542, 41-54.
11. (a) Spinke, J.; Liley, M.; Guder, H.-J.; Angermaier, L.; Knoll, W. Langmuir 1993, 9, 1821-1825.
12. (b) Müller, W.; Ringsdorf, H.; Rump, E.; Wildburg, G.; Zhang, X.; Angermaier, L.; Knoll, W.; Liley, M.; Spinke, J. Science 1993, 262, 1706-1708.
13. Hamachi, I.; Noda, S.; Kunitake, T. J. Am. Chem. Soc. 1991, 113, 9625-9630.
14. Iuliano D. J.; Saavedra, S. S.; Truskey, G. A. J. Biomed. Mater. Res. 1993, 27, 1103-1113.
15. Darst, S. A.; Robertson, C. R.; Berzofsky, J. A. Biophys. J. 1988, 53, 533-539.
16. Lee, C.-S.; Belfort, G. Proc. Natl. Acad. Sci. U.S.A. 1989, 86, 8392-8396.
17. Koyama, K.; Yamaguchi, N.; Miyasaka, T. Science 1994, 265, 762-765.
18. Stayton, P. S.; Ollinger, J. M.; Jiang, M.; Bohn, P. W.; Sligar, S. G. J. Am. Chem. Soc. 1992, 114, 9298-9299.
19. Hong, H.-G.; Bohn, P. W.; Sugar, S. G. Anal. Chem. 1993, 65, 1635-1638.
20. Pachence, J. M.; Amador, S.; Maniara, G.; Vanderkooi, J.; Dutton, P. L.; Blasie, J. K. Biophys. J. 1990, 58, 379-389.
21. Macdonald, I. D. G.; Smith, W. G. Langmuir 1996, 12, 706-713.
22. (a) Walker, D. S.; Hellinga, H. W; Saavedra, S. S.; Reichert, W. M. J. Phys. Chem. 1993, 97, 10217-10222.
23. (b) Lee, J. E; Saavedra, S. S. In Proteins at Interfaces II, Horbett, T. A., Brash, J. L., Eds.; ACS Symposium Series 602; American Chemical Society; Washington, DC, 1995; pp 269-279.
24. Fraaije, J. G. E. M.; Kleijn, J. M.; van der Graaf, M.; Dijt, J. C. Biophys. J. 1990, 57, 965-975.
25. (a) Timbs, M. M.; Thompson, N. L. Biophys. J. 1990, 58, 413-428.
26. (b) Thompson, N. L.; McConnell, H. M.; Burghardt, T. P. Biophys. J. 1984, 46, 739-747.
27. Szabo, A. J. Chem. Phys. 1980, 72, 4620-4626.
28. (a) Wirth, M. J.; Burbage, J. D. Anal. Chem. 1991, 63, 1311-1317.
29. (b) Burbage, J. D.; Wirth, M. J. J. Phys. Chem. 1992, 96, 5943-5948.
30. (c) Wirth, M. J.; Piasecki-Coleman, D. A.; Montgomery, Jr., M. E. Langmuir 1995, 11, 990-995.
31. (a) Bos, M. A.; Kleijn, J. M. Biophys. J. 1995, 68, 2573-2579.
32. (b) Bos, M. A.; Kleijn, J. M. Biophys. J. 1995, 68, 2566-2572.
33. LeGrange, J. D.; Riegler, H. E.; Zurawsky, W. P.; Scarlata, S. F. J. Chem. Phys. 1989, 90, 3838-3842.
34. Edmiston, P. L.; Wood, L. L.; Lee, J. E.; Saavedra, S. S. J. Phys. Chem. 1996, 100, 775-784.
35. Hofrichter, J.; Eaton, W. A. Annu. Rev. Biophys. Bioeng. 1976, 5, 511-560.
36. Saavedra, S. S.; Reichert, W. M. Anal. Chem. 1990, 62, 2251-2256.
37. Reichert, W. M. Crit. Rev. Biocompat. 1989, 5, 173-205.
38. (a) Ruaudel-Teixier, A.; Barraud, A.; Belbeoch, B.; Roulliay, M. Thin Solid Films 1983, 99, 33-40.
39. (b) Dorough, G. D.; Miller, J. R.; Huennekens, F. M. J. Am. Chem. Soc. 1951, 73, 4315-4320.
40. Balachander, N.; Sukenik, C. N. Langmuir 1990, 6, 1621-1627.
41. Margoliash, E.; Frohwirt, N. Biochem. J. 1959, 71, 570-572.
42. (a) Robinson, A. B.; Kamen, M. D. In Structure and Function of Cytochromes; Okunuki, K., Kamen, M. D., Sekuzu, I., Eds.; University Park Press: Baltimore, 1968; pp 383-387.
43. (b) Vanderkooi, J. M.; Adar, F.; Erecinska, M. Eur. J. Biochem. 1976, 64, 381-387.
44. Conjugation With Amine Reactive Probes. technical bulletin; available from Molecular Probes, Eugene, OR.
45. Walker, D. S.; Reichert, W. M.; Berry, C. J. Appl. Spectrosc 1992, 46, 1437-1441.
46. Yang, L.; Saavedra, S. S.; Armstrong, N. R.; Hayes; J. Anal. Chem. 1994, 66, 1254-1263.
47. Yang, L.; Saavedra, S. S. Anal. Chem. 1995, 67, 1307-1314.
48. Lakowicz, J. R. Principles of Fluorescence Spectroscopy, Plenum: New York, 1983; p 120.
49. Gouterman, M.; Stryer, L. J. Chem. Phys. 1962, 37, 2260-2266.
50. (a) Lesieur, P.; Vandevyver, M.; Ruaudel-Teixier, A.; Barraud, A. Thin Solid Films 1988, 159, 315-322.
51. (b) Palacin, S.; Ruaudel-Teixier, A.; Barraud, A. J. Phys. Chem. 1986, 90, 6237-6242.
52. Moore, G. R.; Pettigrew, G. W. Cytochromes c. Evolutionary, Structural, and Physicochemical Aspects; Springer-Verlag: Berlin, 1990; p 24.
53. Lvov, Y.; Ariga, K.; Ichinose, I.; Kunitake, T. J. Am. Chem. Soc. 1995, 117, 6117-6123.
54. (a) Koppenol, W. H.; Margoliash, E. J. Biol. Chem. 1982, 257, 4426-4437.
55. (b) Sankaram, M. B.; Marsh, D. In Protein-Lipid Interactions; Watts, A., Ed.; Elsevier: London, 1993; p 130.
56. See for example: (a) Pachence, J. M.; Blasie, J. K. Biophys. J. 1988, 52, 735-747. (b) Heimburg, T.; Marsh, D. Biophys. J. 1993, 65, 2408-2417 and references therein.
57. See for example: (a) Pachence, J. M.; Blasie, J. K. Biophys. J. 1988, 52, 735-747. (b) Heimburg, T.; Marsh, D. Biophys. J. 1993, 65, 2408-2417 and references therein.
58. σ > 30°. See Figure 6 in ref 24.
59. Fatty acid LB films have been extensively studied and are known to be well ordered on a macroscopic scale. See: (a) Ulman, A. An Introduction to Ultrathin OrganicFilms; Academic: San Diego, 1991. (b) Zasadzinski, J. A.; Viswanathan, R.; Madsen, L.; Garnaes, J.; Schwartz, D. K. Science 1994, 263, 1726-1733.
60. Fatty acid LB films have been extensively studied and are known to be well ordered on a macroscopic scale. See: (a) Ulman, A. An Introduction to Ultrathin OrganicFilms; Academic: San Diego, 1991. (b) Zasadzinski, J. A.; Viswanathan, R.; Madsen, L.; Garnaes, J.; Schwartz, D. K. Science 1994, 263, 1726-1733.
61. See for example: Chen, M; Cassidy, R. M. J. Chromatogr. 1992, 602, 227-234.
62. Ahlers, M.; Müller, W.; Reichert, A.; Ringsdorf, H.; Venzmer, J. Angew. Chem., Int. Ed. Engl. 1990, 29, 1269-1285.