FEBS Letters · 2007 · 83 citations · 14 references
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.
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Genome sequence of the dissimilatory metal ion–reducing bacterium Shewanella oneidensis
John F. Heidelberg, Ian T. Paulsen, Eric Gaidos et al. · Nature Biotechnology · 2002 · 846 citations · Full text
Structure of cytochrome c nitrite reductase
Oliver Einsle, Albrecht Messerschmidt, Petra Stach et al. · Nature · 1999 · 386 citations