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A Simple Proposal That Can Explain the Inactivity of Metal-Substituted Superoxide Dismutases
Abstract
We propose that the apparent catalytic inactivity of Mn- and Fe-substituted superoxide dismutases (SODs) reflects E °s that are either lower (Fe-sub-(Mn)SOD) or higher (Mn-sub-(Fe)SOD) than those of native Fe- or Mn-SODs. In support, we show that the E ° of Fe-sub-(Mn)SOD (Fe substituted into Mn-SOD protein) is −240 mV vs NHE, almost 0.5 V lower than our E ° of 220 mV for Fe-SOD. The E ° of Fe-sub-(Mn)SOD is lower than that of O 2 /O 2 • - and therefore is sufficient to explain Fe-sub-(Mn)SOD's inactivity. Indeed, Fe-sub-(Mn)SOD is shown to be unable to oxidize O 2 • - . Alternate causes of inactivity are ruled out by our demonstration that Fe-sub-(Mn)SOD retains the ability to reduce O 2 • - . Thus, the active site remains active with respect to substrate binding and proton and electron transfer. Finally, we show that Fe-sub-(Mn)SOD's inactivity with respect to O 2 • - oxidation cannot be solely due to competitive inhibition by OH - . Thus, our proposal provides a simple chemical basis for the observed catalytic inactivity of metal-exchanged Mn- or Fe-SODs and suggests that these strongly homologous enzymes may provide important insights into mechanisms of redox midpoint potential tuning in proteins.
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Vincent, A., Thauvin, M., Quévrain, E., Mathieu, E., Layani, S., Seksik, P., Batinic-Haberle, I., Vriz, S., Policar, C., & Delsuc, N. (2021) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2021.111431 · Cited by 58
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Metadata
- Authors
- Vance, C. K., & Miller, A.-F.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 1998-01-01
- Volume
- 120
- Issue
- 3
- Pages
- 461-467
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2022040665
- Cited by
- 179
- References
- 0
- FWCI
- 7.01
- Type
- journal article
- Language
- en
- Open access
- closed
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