ArticleThe Journal of biological chemistry2013
Autoxidation and oxygen binding properties of recombinant hemoglobins with substitutions at the αVal-62 or βVal-67 position of the distal heme pocket.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Gentamicin Targeting Human Hemoglobin Induces Methemoglobin Formation and Decreases Oxygen Affinity: A Molecular Mechanism of Hematologic Toxicity.International journal of molecular sciences · 2026Article
- Protein-Enforced Ligand Environments Reshape Classical Coordination Preferences in Copper Polypyridyl Complexes.Journal of the American Chemical Society · 2026Article
- Oxygen Binding Kinetics and Coordination States of Hemoglobins from Early Land Plants.ACS omega · 2025Article
- Hell's Gate Globin-I fromInternational journal of molecular sciences · 2024Article
- Current Challenges in the Development of Acellular Hemoglobin Oxygen Carriers by Protein Engineering.Shock (Augusta, Ga.) · 2019Review
- Human Hemoglobin Subunit Beta Functions as a Pleiotropic Regulator of RIG-I/MDA5-Mediated Antiviral Innate Immune Responses.Journal of virology · 2019Article
- Molecular basis of hemoglobin adaptation in the high-flying bar-headed goose.PLoS genetics · 2018Article
- Sickle Cell Hemoglobin with Mutation at αHis-50 Has Improved Solubility.The Journal of biological chemistry · 2015Article
- New look at hemoglobin allostery.Chemical reviews · 2015Review
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8 authors.
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Abstract
The E11 valine in the distal heme pocket of either the α- or β-subunit of human adult hemoglobin (Hb A) was replaced by leucine, isoleucine, or phenylalanine. Recombinant proteins were expressed in Escherichia coli and purified for structural and functional studies. (1)H NMR spectra were obtained for the CO and deoxy forms of Hb A and the mutants. The mutations did not disturb the α1β2 interface in either form, whereas the H-bond between αHis-103 and βGln-131 in the α1β1 interfaces of the deoxy α-subunit mutants was weakened. Localized structural changes in the mutated heme pocket were detected for the CO form of recombinant Hb (rHb) (αV62F), rHb (βV67I), and rHb (βV67F) compared with Hb A. In the deoxy form the proximal histidyl residue in the β-subunit of rHb (βV67F) has been altered. Furthermore, the interactions between the porphyrin ring and heme pocket residues have been perturbed in rHb (αV62I), rHb (αV62F), and rHb (βV67F). Functionally, the oxygen binding affinity (P50), cooperativity (n50), and the alkaline Bohr Effect of the three α-subunit mutants and rHb (βV67L) are similar to those of Hb A. rHb (βV67I) and rHb (βV67F) exhibit low and high oxygen affinity, respectively. rHb (βV67F) has P50 values lower that those reported for rHb (αL29F), a B10 mutant studied previously in our laboratory (Wiltrout, M. E., Giovannelli, J. L., Simplaceanu, V., Lukin, J. A., Ho, N. T., and Ho, C. (2005) Biochemistry 44, 7207-7217). These E11 mutations do not slow down the autoxidation and azide-induced oxidation rates of the recombinant proteins. Results from this study provide new insights into the roles of E11 mutants in the structure-function relationship in hemoglobin.
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