Mind the gap: diversity and reactivity relationships among multihaem cytochromes of the MtrA/DmsE family
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 Dms...
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| Format: | Article |
| Language: | en_US |
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Portland Press
2014
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| Online Access: | http://hdl.handle.net/1721.1/83905 https://orcid.org/0000-0001-5486-2755 |
| _version_ | 1811078070717644800 |
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| author | Bewley, Kathryn D. Firer-Sherwood, Mackenzie A. Mock, Jee‑Young Ando, Nozomi Elliott, Sean J. Drennan, Catherine L |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Bewley, Kathryn D. Firer-Sherwood, Mackenzie A. Mock, Jee‑Young Ando, Nozomi Elliott, Sean J. Drennan, Catherine L |
| author_sort | Bewley, Kathryn D. |
| collection | MIT |
| description | 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. |
| first_indexed | 2024-09-23T10:52:55Z |
| format | Article |
| id | mit-1721.1/83905 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T10:52:55Z |
| publishDate | 2014 |
| publisher | Portland Press |
| record_format | dspace |
| spelling | mit-1721.1/839052022-09-27T15:39:39Z Mind the gap: diversity and reactivity relationships among multihaem cytochromes of the MtrA/DmsE family Bewley, Kathryn D. Firer-Sherwood, Mackenzie A. Mock, Jee‑Young Ando, Nozomi Elliott, Sean J. Drennan, Catherine L Massachusetts Institute of Technology. Department of Biology Massachusetts Institute of Technology. Department of Chemistry Drennan, Catherine L. Ando, Nozomi Drennan, Catherine L. 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. National Science Foundation (U.S.) (Grant MCB 0546323) National Science Foundation (U.S.) (Grant CHE 0840418) Research Corporation for Science Advancement (Scialog Award) National Institutes of Health (U.S.) (Grant F32GM904862) 2014-01-13T18:24:00Z 2014-01-13T18:24:00Z 2012-12 2012-04 Article http://purl.org/eprint/type/JournalArticle 0300-5127 1470-8752 http://hdl.handle.net/1721.1/83905 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. https://orcid.org/0000-0001-5486-2755 en_US http://dx.doi.org/10.1042/bst20120106 Biochemical Society Transactions Creative Commons Attribution-Noncommercial-Share Alike 3.0 http://creativecommons.org/licenses/by-nc-sa/3.0/ application/pdf Portland Press Prof. Drennan via Erja Kajosalo |
| spellingShingle | Bewley, Kathryn D. Firer-Sherwood, Mackenzie A. Mock, Jee‑Young Ando, Nozomi Elliott, Sean J. Drennan, Catherine L Mind the gap: diversity and reactivity relationships among multihaem cytochromes of the MtrA/DmsE family |
| title | Mind the gap: diversity and reactivity relationships among multihaem cytochromes of the MtrA/DmsE family |
| title_full | Mind the gap: diversity and reactivity relationships among multihaem cytochromes of the MtrA/DmsE family |
| title_fullStr | Mind the gap: diversity and reactivity relationships among multihaem cytochromes of the MtrA/DmsE family |
| title_full_unstemmed | Mind the gap: diversity and reactivity relationships among multihaem cytochromes of the MtrA/DmsE family |
| title_short | Mind the gap: diversity and reactivity relationships among multihaem cytochromes of the MtrA/DmsE family |
| title_sort | mind the gap diversity and reactivity relationships among multihaem cytochromes of the mtra dmse family |
| url | http://hdl.handle.net/1721.1/83905 https://orcid.org/0000-0001-5486-2755 |
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