Interruption and time-resolution of catalysis by a flavoenzyme using fast scan protein film voltammetry [4]

Journal of the American Chemical Society

Volumn 122, Issue 27, 2000, Pages 6494-6495

  Jones, Anne K ^a   Camba, Raúl ^a   Reid, Graeme A ^b   Chapman, Stephen K ^b   Armstrong, Fraser A ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF EDINBURGH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

FLAVOPROTEIN;

CATALYSIS; CATALYST; ELECTRON TRANSPORT; ENZYME SUBSTRATE COMPLEX; LETTER; POTENTIOMETRY; REACTION ANALYSIS;

EID: 0034641342     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja000848n     Document Type: Letter

References (21)

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2. (b) Easter, M. C.; Gibson, D. M.; Ward, F. B. J. Gen. Microbiol. 1983, 129, 3689-3696.
3. (c) Pealing, S. L.; Cheeseman, M. R.; Reid, G. A.; Thomson, A. J.; Ward, B.; Chapman, S. K. Biochemistry 1995, 34. 6153-6158.
4. Taylor, P.; Pealing, S. L.; Reid, G. A.; Chapman, S. K.; Walkinshaw, M. D. Nat. Struct. Biol. 1999, 6, 1108-1112.
5. Turner, K. L.; Doherty, M. K.; Heering, H. A.; Armstrong, F. A.; Reid, G. A.; Chapman, S. K. Biochemistry 1999, 38, 3302-3309.
6. Laviron, E. Electroanalytical Chemistry; Bard, A. J., Ed.; Marcel Dekker: New York, 1982; Vol. 12, pp 53-157.
7. (a) Sucheta, A.; Cammack, R.; Weiner, J.; Armstrong, F. A. Biochemistry 1993, 32, 5455-5465.
8. (b) Armstrong, F. A.; Heering, H. A.; Hirst, J. Chem. Soc. Rev. 1997, 26, 169-179.
9. (c) Heering, H. A.; Weiner, J. H.; Armstrong, F. A. J. Am. Chem. Soc. 1997, 119, 11628-11638.
10. Protein film fast scan cyclic voltammetry is described in: (a) Hirst, J.; Armstrong, F. A. Anal. Chem. 1998, 70, 5062-5071. (b) Hirst, J.; Duff, J. L. C.; Jameson, G. N. L.; Kemper, M. A.; Burgess, B. K.; Armstrong, F. A. J. Am. Chem. Soc. 1998, 120, 7085-7094. (c) Hirst, J.; Jameson, G. N. L.; Allen, J. W. A.; Armstrong, F. A. J. Am. Chem. Soc. 1998, 120, 11994-11999. For fast scan cyclic voltammetry of small-molecule monolayers, see, for example: (d) Weber, K.; Creager, S. E. Anal. Chem. 1994, 66, 3164-3172.
11. Protein film fast scan cyclic voltammetry is described in: (a) Hirst, J.; Armstrong, F. A. Anal. Chem. 1998, 70, 5062-5071. (b) Hirst, J.; Duff, J. L. C.; Jameson, G. N. L.; Kemper, M. A.; Burgess, B. K.; Armstrong, F. A. J. Am. Chem. Soc. 1998, 120, 7085-7094. (c) Hirst, J.; Jameson, G. N. L.; Allen, J. W. A.; Armstrong, F. A. J. Am. Chem. Soc. 1998, 120, 11994-11999. For fast scan cyclic voltammetry of small-molecule monolayers, see, for example: (d) Weber, K.; Creager, S. E. Anal. Chem. 1994, 66, 3164-3172.
12. Protein film fast scan cyclic voltammetry is described in: (a) Hirst, J.; Armstrong, F. A. Anal. Chem. 1998, 70, 5062-5071. (b) Hirst, J.; Duff, J. L. C.; Jameson, G. N. L.; Kemper, M. A.; Burgess, B. K.; Armstrong, F. A. J. Am. Chem. Soc. 1998, 120, 7085-7094. (c) Hirst, J.; Jameson, G. N. L.; Allen, J. W. A.; Armstrong, F. A. J. Am. Chem. Soc. 1998, 120, 11994-11999. For fast scan cyclic voltammetry of small-molecule monolayers, see, for example: (d) Weber, K.; Creager, S. E. Anal. Chem. 1994, 66, 3164-3172.
13. Protein film fast scan cyclic voltammetry is described in: (a) Hirst, J.; Armstrong, F. A. Anal. Chem. 1998, 70, 5062-5071. (b) Hirst, J.; Duff, J. L. C.; Jameson, G. N. L.; Kemper, M. A.; Burgess, B. K.; Armstrong, F. A. J. Am. Chem. Soc. 1998, 120, 7085-7094. (c) Hirst, J.; Jameson, G. N. L.; Allen, J. W. A.; Armstrong, F. A. J. Am. Chem. Soc. 1998, 120, 11994-11999. For fast scan cyclic voltammetry of small-molecule monolayers, see, for example: (d) Weber, K.; Creager, S. E. Anal. Chem. 1994, 66, 3164-3172.
14. -1 Polymyxin B sulfate (Sigma) as coadsorbate to stabilize the film. Solutions of fumaric acid (Fluka, 99.5%) were prepared in the mixed buffer system, and the pH was adjusted using NaOH. All potentials are reported with reference to the standard hydrogen electrode (SHE) based on a potential of 242 mV for SCE at 20 °C.
15. 10 °C is a physiological temperature for Shewanella frigidimarina (habitat, North Sea).
16. This attenuation is remarkably small, considering the very large dynamic range: many smaller proteins show greater decreases in normalized peak area as the scan rate is raised. See Hirst et al. (ref 6a).
17. For an account of the use of rotating disc electrodes, see: Instrumental Methods in Electrochemistry; Southampton Electrochemistry Group: Ellis Horwood, 1993; Chapter 4.
18. Britz, D. Digital Simulation in Electrochemistry, 2nd ed.; Springer-Verlag: Berlin, 1988.
19. Observability of non-catalytic electron transfer is judged from the first appearance of local extrema in the voltammogram.
20. Page, C. C.; Moser, C. C.; Chen, X. X.; Dutton, P. L. Nature 1999, 402, 47-52.
21. 3 may therefore be considered as an example of an enzyme that is naturally "wired" to display electroactivity at an electrode. See: Heller, A. Acc Chem. Res. 1990, 23, 128-134.