ArticleBiochemistry2011
Crystallographic trapping of heme loss intermediates during the nitrite-induced degradation of human hemoglobin.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 27 citations in OpenAlex.
- Nitric Oxide Binding Geometry in Heme-Proteins: Relevance for Signal Transduction.Antioxidants (Basel, Switzerland) · 2024Review
- Article
- Dynamics based clustering of globin family members.PloS one · 2018Article
- Integrative and comparative reproductive biology: From alligators to xenobiotics.General and comparative endocrinology · 2016Review
- Crystallographic characterization of the nitric oxide derivative of R-state human hemoglobin.Nitric oxide : biology and chemistry · 2014Article
- Leghemoglobin green derivatives with nitrated hemes evidence production of highly reactive nitrogen species during aging of legume nodules.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Heme is an important cofactor in a large number of essential proteins and is often involved in small molecule binding and activation. Loss of heme from proteins thus negatively affects the function of these proteins but is also an important component of iron recycling. The characterization of intermediates that form during the loss of heme from proteins has been problematic, in a large part, because of the instability of such intermediates. We have characterized, by X-ray crystallography, three compounds that form during the nitrite-induced degradation of human α(2)β(2) hemoglobin (Hb). The first is an unprecedented complex that exhibits a large β heme displacement of 4.8 Å toward the protein exterior; the heme displacement is stabilized by the binding of the distal His residue to the heme Fe, which in turn allows for the unusual binding of an exogenous ligand on the proximal face of the heme. We have also structurally characterized complexes that display regiospecific nitration of the heme at the 2-vinyl position; we show that heme nitration is not a prerequisite for heme loss. Our results provide structural insight into a possible pathway for nitrite-induced loss of heme from human Hb.
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Registered trials
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