Cytochrome c nitrite reductase from Wolinella succinogenes -: Structure at 1.6 Å resolution, inhibitor binding, and heme-packing motifs

被引:159
作者
Einsle, O
Stach, P
Messerschmidt, A
Simon, J
Kröger, A
Huber, R
Kroneck, PMH
机构
[1] Univ Konstanz, Math Naturwissensch Sekt, Fachbereich Biol, D-78457 Constance, Germany
[2] Max Planck Inst Biochem, Abt Strukturforsch, D-82152 Martinsried, Germany
[3] Goethe Univ Frankfurt, Inst Mikrobiol, D-60439 Frankfurt, Germany
关键词
D O I
10.1074/jbc.M006188200
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
Cytochrome c nitrite reductase catalyzes the 6-electron reduction of nitrite to ammonia. This second part of the respiratory pathway of nitrate ammonification is a key step in the biological nitrogen cycle. The x-ray structure of the enzyme from the epsilon -proteobacterium Wolinella succinogenes has been solved to a resolution of 1.6 Angstrom It is a pentaheme c-type cytochrome whose heme groups are packed in characteristic motifs that also occur in other multiheme cytochromes. Structures of W. succinogenes nitrite reductase have been obtained with water bound to the active site heme iron as well as complexes with two inhibitors, sulfate and azide, whose binding modes and inhibitory functions differ significantly. Cytochrome c nitrite reductase is part of a highly optimized respiratory system found in a wide range of Gram-negative bacteria. It reduces both anionic and neutral substrates at the distal side of a lysine-coordinated high-spin heme group, which is accessible through two different channels, allowing for a guided flow of reaction educt and product. Based on sequence comparison and secondary structure prediction, we have demonstrated that cytochrome c nitrite reductases constitute a protein family of high structural similarity.
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页码:39608 / 39616
页数:9
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