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Abstract / Description of output
We have isolated a soluble cytochrome from Shewanella oneidensis that contains eight covalently attached heme groups and determined its crystal structure. One of these hemes exhibits novel ligation of the iron atom by the epsilon-amino group of a lysine residue, despite its attachment via a typical CXXCH motif. This heme is most likely the active site for tetrathionate reduction, a reaction catalyzed efficiently by this enzyme.
Original language | English |
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Pages (from-to) | 1023-1024 |
Number of pages | 2 |
Journal | Nature Structural & Molecular Biology |
Volume | 11 |
Issue number | 10 |
DOIs | |
Publication status | Published - Oct 2004 |
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Dive into the research topics of 'Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation'. 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