Structural highlights
Function
Q8E9W8_SHEON
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation.,Mowat CG, Rothery E, Miles CS, McIver L, Doherty MK, Drewette K, Taylor P, Walkinshaw MD, Chapman SK, Reid GA Nat Struct Mol Biol. 2004 Oct;11(10):1023-4. Epub 2004 Sep 7. PMID:15361860[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mowat CG, Rothery E, Miles CS, McIver L, Doherty MK, Drewette K, Taylor P, Walkinshaw MD, Chapman SK, Reid GA. Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation. Nat Struct Mol Biol. 2004 Oct;11(10):1023-4. Epub 2004 Sep 7. PMID:15361860 doi:10.1038/nsmb827
