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High-Affinity Binding and Direct Electron Transfer to Solid Metals by the Shewanella oneidensis MR-1 Outer Membrane c-type Cytochrome OmcA
Abstract
The purified outer membrane bacterial protein OmcA binds densely to the surface of hematite (Fe2O3), permitting direct electron transfer to this solid mineral to reduce Fe (III) with an electron flux of about 1013 electrons /cm2/s. In the presence of hematite, there is a substantial increase in the amplitude of internal protein motions that correlate with metal reduction. Binding is highly favorable, with a partition coefficient of approximately 2 x 105 (DeltaGo' = -28 kJ/mol), where approximately 1014 OmcA proteins bind per cm2 to the solid metal surface, indicating the utility of using purified OmcA in the construction of a biofuel cell.
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Cited by
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Self-citationYong, Y.-C., Dong, X.-C., Chan-Park, M. B., Song, H., & Chen, P. (2012) · ACS Nano · doi:10.1021/nn204656d · Cited by 565
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Yu, H., Irie, H., Shimodaira, Y., Hosogi, Y., Kuroda, Y., Miyauchi, M., & Hashimoto, K. (2010) · The Journal of Physical Chemistry C · doi:10.1021/jp1071956 · Cited by 364
Metadata
- Authors
- Xiong, Y., Shi, L., Chen, B., Mayer, M. U., Lower, B. H., Londer, Y., Bose, S., Hochella, M. F., Fredrickson, J. K., & Squier, T. C.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2006-10-11
- Volume
- 128
- Issue
- 43
- Pages
- 13978-13979
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2059642862
- Cited by
- 221
- References
- 0
- FWCI
- 19.07
- Type
- journal article
- Language
- en
- Open access
- closed
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- Xiong, Y., Shi, L., Chen, B., Mayer, M. U., Lower, B. H., Londer, Y., Bose, S., Hochella, M. F., Fredrickson, J. K., & Squier, T. C. (2006). High-Affinity Binding and Direct Electron Transfer to Solid Metals by the Shewanella oneidensis MR-1 Outer Membrane c-type Cytochrome OmcA. Journal of the American Chemical Society. https://doi.org/10.1021/ja063526d
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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