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Mind the gap: diversity and reactivity relationships among multihaem cytochromes of the MtrA/DmsE family.
- Source :
-
Biochemical Society transactions [Biochem Soc Trans] 2012 Dec 01; Vol. 40 (6), pp. 1268-73. - Publication Year :
- 2012
-
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.
- Subjects :
- Bacterial Proteins chemistry
Bacterial Proteins metabolism
Bacterial Proteins physiology
Cytochrome c Group chemistry
Cytochrome c Group metabolism
Dimethyl Sulfoxide metabolism
Electron Transport
Heme chemistry
Iron-Sulfur Proteins chemistry
Iron-Sulfur Proteins metabolism
Iron-Sulfur Proteins physiology
Models, Molecular
Oxidation-Reduction
Oxidoreductases chemistry
Oxidoreductases metabolism
Oxidoreductases physiology
Sequence Homology, Amino Acid
Shewanella enzymology
Cytochrome c Group physiology
Periplasm enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1470-8752
- Volume :
- 40
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Biochemical Society transactions
- Publication Type :
- Academic Journal
- Accession number :
- 23176466
- Full Text :
- https://doi.org/10.1042/BST20120106