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Abstract / Description of output
A c-type cytochrome from Shewanella oneidensis MR-1, containing eight hemes, has been previously designated as an octaheme tetrathionate reductase (OTR). The structure of OTR revealed that the active site contains an unusual lysine-ligated heme, despite the presence of a CXXCH motif in the sequence that would predict histidine ligation. This lysine ligation has been previously observed only in the pentaheme nitrite reductases, suggesting that OTR may have a possible role in nitrite reduction. We have now shown that OTR is an efficient nitrite and hydroxylamine reductase and that ammonium ion is the product. These results indicate that OTR may have a role in the biological nitrogen cycle.
Original language | English |
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Pages (from-to) | 3805-3808 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 581 |
Issue number | 20 |
Early online date | 16 Jul 2007 |
DOIs | |
Publication status | Published - Aug 2007 |
Keywords / Materials (for Non-textual outputs)
- Octaheme tetrathionate reductase
- Cytochrome c
- Nitrite
- Hydroxylamine
- Nitrogen cycle
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Dive into the research topics of 'An octaheme c-type cytochrome from Shewanella oneidensis can reduce nitrite and hydroxylamine'. Together they form a unique fingerprint.Projects
- 1 Finished
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Molecular enzymology of a novel tetrathionate reductase
Reid, G. & Chapman, S.
1/10/03 → 30/09/06
Project: Research