Cytochrome c Nitrite Reductase from Wolinella succinogenes

• Published in: The Journal of biological chemistry 2000-12, Vol.275 (50), p.39608-39616
• Main Authors: Einsle, Oliver, Stach, Petra, Messerschmidt, Albrecht, Simon, Jörg, Kröger, Achim, Huber, Robert, Kroneck, Peter M.H.
• Format: Article
• Language: English
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.M006188200

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 ε-proteobacterium Wolinella succinogenes has been solved to a resolution of 1.6 Å. It is a pentahemec-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 cnitrite 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 cytochromec nitrite reductases constitute a protein family of high structural similarity.