ArticleBiophysical journal2006
Sulfide-binding hemoglobins: Effects of mutations on active-site flexibility.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Chemical Biology of HChemical reviews · 2018Review
- Molecular Cloning and Characterization of a (Lys)6-Tagged Sulfide-Reactive Hemoglobin I from Lucina pectinata.Molecular biotechnology · 2015Article
- Hydrogen sulfide activation in hemeproteins: the sulfheme scenario.Journal of inorganic biochemistry · 2014Review
- Hydrogen sulfide and hemeproteins: knowledge and mysteries.Antioxidants & redox signaling · 2011Review
- Degradation of sulfide by dehaloperoxidase-hemoglobin from Amphitrite ornata.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Article
- Interactions of multiple gas-transducing systems: hallmarks and uncertainties of CO, NO, and H2S gas biology.Antioxidants & redox signaling · 2010Review
- Factors controlling the reactivity of hydrogen sulfide with hemeproteins.Biochemistry · 2009Article
- Effects of active site mutations in haemoglobin I from Lucina pectinata: a molecular dynamic study.Molecular simulation · 2008Article
- Structure and ligand selection of hemoglobin II from Lucina pectinata.The Journal of biological chemistry · 2008Article
- Computational biology in Argentina.PLoS computational biology · 2007Review
Corrections and comments
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Authors and funding
6 authors at 5 institutions in 3 countries.
Funding
Abstract
The dynamics of Hemoglobin I (HbI) from the clam Lucina pectinata, from wild-type sperm whale (SW) myoglobin, and from the L29F/H64Q/V68F triple mutant of SW, both unligated and bound to hydrogen sulfide (H2S), have been studied in molecular dynamics simulations. Features that account for differences in H2S affinity among the three have been examined. Our results verify the existence of an unusual heme rocking motion in unligated HbI that can promote the entrance of large ligands such as H2S. The FQF-mutant partially reproduces the amplitude and relative orientation of the motion of HbI's heme group. Therefore, besides introducing favorable electrostatic interactions with H2S, the three mutations in the distal pocket change the dynamic properties of the heme group. The active-site residues Gln-64(E7), Phe-43(CD1), and His-93(F8) are also shown to be more flexible in unligated HbI than in FQF-mutant and SW. Further contributions to H2S affinity come from differences in hydrogen bonding between the heme propionate groups and nearby amino acid residues.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.