The Nitrite Anion Binds to Human Hemoglobin via the Uncommon O-Nitrito Mode
Biochemistry2008Vol. 47(32), pp. 8247–8249
Citations Over TimeTop 10% of 2008 papers
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.
Related Papers
- → Nitrite utilization in the roots of higher plants(1980)14 cited
- → Nitrite reduction in Rhizobium ?hedysari? strain HCNT 1(1986)41 cited
- → Nitrite reduction in Bacteroids of Rhizobium ?hedysari? strain HCNT 1(1988)30 cited
- → ChemInform Abstract: FERRIC ION SEQUESTERING AGENTS. 10. SELECTIVITY OF SULFONATED POLY(CATECHOYLAMIDES) FOR FERRIC ION(1982)7 cited
- The Effect of Oxygen Supply on Nitrite Reduction by Tallgrass Prairie Soil Bacteria(2016)