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An octaheme c ‐type cytochrome from Shewanella oneidensis can reduce nitrite and hydroxylamine
Author(s) -
Atkinson Sally J.,
Mowat Christopher G.,
Reid Graeme A.,
Chapman Stephen K.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.07.005
Subject(s) - shewanella oneidensis , hydroxylamine , chemistry , nitrite , biochemistry , nitrite reductase , stereochemistry , biology , organic chemistry , bacteria , nitrate , genetics
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.