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. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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Natl Res Council Canada, Biotechnol Res Inst, Montreal, PQ H4P 2R2, CanadaNatl Res Council Canada, Biotechnol Res Inst, Montreal, PQ H4P 2R2, Canada
Perreault, Nancy N.
Crocker, Fiona H.
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USA, Engn Res & Dev Ctr, Vicksburg, MS 39180 USANatl Res Council Canada, Biotechnol Res Inst, Montreal, PQ H4P 2R2, Canada
Crocker, Fiona H.
Indest, Karl J.
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USA, Engn Res & Dev Ctr, Vicksburg, MS 39180 USANatl Res Council Canada, Biotechnol Res Inst, Montreal, PQ H4P 2R2, Canada
Indest, Karl J.
Hawari, Jalal
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Natl Res Council Canada, Biotechnol Res Inst, Montreal, PQ H4P 2R2, CanadaNatl Res Council Canada, Biotechnol Res Inst, Montreal, PQ H4P 2R2, Canada