Cytochrome c nitrite reductase

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== Structural highlights ==
== Structural highlights ==
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In the ''Wolinella succinogenes'' ccNiR structure the substrate NO2 binds to the Fe+3 atom of the heme group and makes hydrogen bonds to side chains of residues R114 and H277<ref>PMID:12296741</ref>.
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In the ''Wolinella succinogenes'' ccNiR structure the substrate NO<sub>2</sub> binds to the Fe+3 atom of the heme group and makes hydrogen bonds to side chains of residues R114 and H277<ref>PMID:12296741</ref>.
</StructureSection>
</StructureSection>

Revision as of 11:45, 12 January 2020

Cytochrome c nitrite reductase with 5 heme groups complex with NO2, acetate Ca+2 ion (green) and Y+3 ion (cyan) (PDB code 2e80)

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3D structures of cytochrome c nitrite reductase

Updated on 12-January-2020

References

  1. Einsle O, Messerschmidt A, Stach P, Bourenkov GP, Bartunik HD, Huber R, Kroneck PM. Structure of cytochrome c nitrite reductase. Nature. 1999 Jul 29;400(6743):476-80. PMID:10440380 doi:10.1038/22802
  2. Einsle O, Messerschmidt A, Huber R, Kroneck PM, Neese F. Mechanism of the six-electron reduction of nitrite to ammonia by cytochrome c nitrite reductase. J Am Chem Soc. 2002 Oct 2;124(39):11737-45. PMID:12296741

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Alexander Berchansky, Michal Harel

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