1fs7
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CYTOCHROME C NITRITE REDUCTASE FROM WOLINELLA SUCCINOGENES
OverviewOverview
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 A. 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.
About this StructureAbout this Structure
1FS7 is a Single protein structure of sequence from Wolinella succinogenes with CA, Y1, ACT and HEM as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Cytochrome c nitrite reductase from Wolinella succinogenes. Structure at 1.6 A resolution, inhibitor binding, and heme-packing motifs., Einsle O, Stach P, Messerschmidt A, Simon J, Kroger A, Huber R, Kroneck PM, J Biol Chem. 2000 Dec 15;275(50):39608-16. PMID:10984487
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