The nitrite anion binds to human hemoglobin via the uncommon O-nitrito mode

Biochemistry. 2008 Aug 12;47(32):8247-9. doi: 10.1021/bi801015c. Epub 2008 Jul 17.

Abstract

The nitrite anion is known to oxidize and degrade hemoglobin (Hb). Recent literature reports suggest a nitrite reductase activity for Hb, converting nitrite into nitric oxide. Surprisingly, no structural information about Hb-nitrite interactions has been reported. We have determined the crystal structure of the ferric Hb-nitrite complex at 1.80 A resolution. The nitrite ligand adopts the uncommon O-nitrito binding mode. In addition, the nitrito conformations in the alpha and beta subunits are different, reflecting subtle effects of the distal His in orienting the nitrite ligand in the O-nitrito binding mode.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Adult
  • Anions / chemistry
  • Anions / metabolism*
  • Binding Sites
  • Crystallography, X-Ray
  • Hemoglobins / chemistry
  • Hemoglobins / metabolism*
  • Humans
  • Nitrites / chemistry
  • Nitrites / metabolism*
  • Protein Binding

Substances

  • Anions
  • Hemoglobins
  • Nitrites

Associated data

  • PDB/3D7O