Mind the gap: diversity and reactivity relationships among multihaem cytochromes of the MtrA/DmsE family
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Drennan_DmsE_042412_Final.pdf
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Author(s)
Bewley, Kathryn D.
Firer-Sherwood, Mackenzie A.
Mock, Jee‑Young
Ando, Nozomi
Elliott, Sean J.
Drennan, Catherine L
Date Issued
December 2012
Journal
Biochemical Society Transactions
Publisher
Portland Press
Citation
Bewley, Kathryn D., Mackenzie A. Firer‑Sherwood, Jee‑Young Mock, Nozomi Ando, Catherine L. Drennan, and Sean J. Elliott. “Mind the gap: diversity and reactivity relationships among multihaem cytochromes of the MtrA/DmsE family.” Biochemical Society Transactions 40, no. 6 (December 1, 2012): 1268-1273.
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Author's final manuscript
Abstract
Shewanella oneidensis MR-1 has the ability to use many external terminal electron acceptors during anaerobic respiration, such as DMSO. The pathway that facilitates this electron transfer includes the decahaem cytochrome DmsE, a paralogue of the MtrA family of decahaem cytochromes. Although both DmsE and MtrA are decahaem cytochromes implicated in the long-range electron transfer across a ~300 Å (1 Å=0.1 nm) wide periplasmic ‘gap’, MtrA has been shown to be only 105 Å in maximal length. In the present paper, DmsE is further characterized via protein film voltammetry, revealing that the electrochemistry of the DmsE haem cofactors display macroscopic potentials lower than those of MtrA by 100 mV. It is possible this tuning of the redox potential of DmsE is required to shuttle electrons to the outer-membrane proteins specific to DMSO reduction. Other decahaem cytochromes found in S. oneidensis, such as the outer-membrane proteins MtrC, MtrF and OmcA, have been shown to have electrochemical properties similar to those of MtrA, yet possess a different evolutionary relationship.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Massachusetts Institute of Technology. Department of Chemistry
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DOI of Published Version
https://doi.org/10.1042/bst20120106
