An octaheme c-type cytochrome from Shewanella oneidensis can reduce nitrite and hydroxylamine

被引:66
作者
Atkinson, Sally J.
Mowat, Christopher G.
Reid, Graeme A.
Chapman, Stephen K.
机构
[1] Univ Edinburgh, Sch Chem, EaStCHEM, Edinburgh EH9 3JJ, Midlothian, Scotland
[2] Univ Edinburgh, Inst Struct & Mol Biol, Edinburgh EH9 3JR, Midlothian, Scotland
基金
英国生物技术与生命科学研究理事会;
关键词
octaheme tetrathionate reductase; cytochrome c; nitrite; hydroxylamine; nitrogen cycle;
D O I
10.1016/j.febslet.2007.07.005
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:3805 / 3808
页数:4
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