The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Enzyme Electrokinetics: Using Protein Film Voltammetry To Investigate Redox Enzymes and Their Mechanisms
Abstract
Protein film voltammetry is a relatively new approach to studying redox enzymes, the concept being that a sample of a redox protein is configured as a film on an electrode and probed by a variety of electrochemical techniques. The enzyme molecules are bound at the electrode surface in such a way that there is fast electron transfer and complete retention of the chemistry of the active site that is observed in more conventional experiments. Modulations of the electrode potential or catalytic turnover result in the movement of electrons to, from, and within the enzyme; this is detected as a current that varies in characteristic ways with time and potential. Henceforth, the potential dimension is introduced into enzyme kinetics. The presence of additional intrinsic redox centers for providing fast intramolecular electron transfer between a buried active site and the protein surface is an important factor. Centers which carry out cooperative two-electron transfer, most obviously flavins, produce a particularly sharp signal that allows them to be observed, even as transient states, when spectroscopic methods are not useful. High catalytic activity produces a large amplification of the current, and useful information can be obtained even if the coverage on the electrode is low. Certain enzymes display optimum activity at a particular potential, and this can be both mechanistically informative and physiologically relevant. This paper outlines the principles of protein film voltammetry by discussing some recent results from this laboratory.
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Citations
Cites
Reaction of complex metalloproteins studied by protein-film voltammetry
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Interpreting the Catalytic Voltammetry of Electroactive Enzymes Adsorbed on Electrodes
Heering, H. A., Hirst, J., & Armstrong, F. A. (1998) · The Journal of Physical Chemistry B · doi:10.1021/jp981023r · Cited by 148
Self-citationHirst, J., Sucheta, A., Ackrell, B. A. C., & Armstrong, F. A. (1996) · Journal of the American Chemical Society · doi:10.1021/ja9534361 · Cited by 115
Self-citationHeering, H. A., Weiner, J. H., & Armstrong, F. A. (1997) · Journal of the American Chemical Society · doi:10.1021/ja9723242 · Cited by 105
Self-citationA Voltammetric Study of Interdomain Electron Transfer within Sulfite Oxidase
Elliott, S. J., McElhaney, A. E., Feng, C., Enemark, J. H., & Armstrong, F. A. (2002) · Journal of the American Chemical Society · doi:10.1021/ja027776f · Cited by 93
Self-citationAngove, H. C., Cole, J. A., Richardson, D. J., & Butt, J. N. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200495200 · Cited by 91
Detection and interpretation of redox potential optima in the catalytic activity of enzymes
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Cited by
The mononuclear molybdenum enzymes
Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738
Enzymes as Working or Inspirational Electrocatalysts for Fuel Cells and Electrolysis
Cracknell, J. A., Vincent, K. A., & Armstrong, F. A. (2008) · Chemical Reviews · doi:10.1021/cr0680639 · Cited by 988
Self-citationDirect Electrochemistry of Redox Enzymes as a Tool for Mechanistic Studies
Léger, C., & Bertrand, P. (2008) · Chemical Reviews · doi:10.1021/cr0680742 · Cited by 783
Self-citationReversible interconversion of carbon dioxide and formate by an electroactive enzyme
Reda, T., Plugge, C. M., Abram, N. J., & Hirst, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801290105 · Cited by 561
Liu, H., Duan, C., Yang, C., Shen, W., Wang, F., & Zhu, Z. (2015) · Sensors and Actuators B: Chemical · doi:10.1016/j.snb.2015.04.090 · Cited by 475
Metadata
- Authors
- Léger, C., Elliott, S. J., Hoke, K. R., Jeuken, L. J. C., Jones, A. K., & Armstrong, F. A.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2003-07-01
- Volume
- 42
- Issue
- 29
- Pages
- 8653-8662
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2019237646
- Cited by
- 289
- References
- 10
- FWCI
- 16.42
- Type
- journal article
- Language
- en
- Open access
- closed
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