期刊
BIOCHEMISTRY
卷 47, 期 32, 页码 8247-8249出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi801015c
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资金
- NIGMS NIH HHS [GM 064476] Funding Source: Medline
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 angstrom 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.
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