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

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

Author information

1
Department of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, USA.

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.

PMID:
18630930
DOI:
10.1021/bi801015c
[Indexed for MEDLINE]

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