ArticleComparative biochemistry and physiology. Part A, Molecular & integrative physiology2012
Oxygenation properties and oxidation rates of mouse hemoglobins that differ in reactive cysteine content.
Article in Comparative biochemistry and physiology. Part A, Molecular & integrative physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 25 citations in OpenAlex.
- Ancestral β-globin gene haplotypes modify β-thalassemia severity in a mouse model.Blood advances · 2024Article
- Red Blood Cell-Mediated S-Nitrosohemoglobin-Dependent Vasodilation: Lessons Learned from a β-Globin Cys93 Knock-In Mouse.Antioxidants & redox signaling · 2021Review
- Article
- Site-directed mutagenesis of cysteine residues alters oxidative stability of fetal hemoglobin.Redox biology · 2018Article
- Gene Turnover and Diversification of the α- and β-Globin Gene Families in Sauropsid Vertebrates.Genome biology and evolution · 2018Article
- Regulation of blood oxygen transport in hibernating mammals.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2017Review
- Gene Duplication and Evolutionary Innovations in Hemoglobin-Oxygen Transport.Physiology (Bethesda, Md.) · 2016Review
- Convergent Evolution of Hemoglobin Function in High-Altitude Andean Waterfowl Involves Limited Parallelism at the Molecular Sequence Level.PLoS genetics · 2015Article
- Contribution of a mutational hot spot to hemoglobin adaptation in high-altitude Andean house wrens.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Oxygenation properties and isoform diversity of snake hemoglobins.American journal of physiology. Regulatory, integrative and comparative physiology · 2015Article
- Intraspecific polymorphism, interspecific divergence, and the origins of function-altering mutations in deer mouse hemoglobin.Molecular biology and evolution · 2015Article
- Epistasis constrains mutational pathways of hemoglobin adaptation in high-altitude pikas.Molecular biology and evolution · 2015Article
- Integrating evolutionary and functional tests of adaptive hypotheses: a case study of altitudinal differentiation in hemoglobin function in an Andean Sparrow, Zonotrichia capensis.Molecular biology and evolution · 2014Article
- Adaptive phylogeography: functional divergence between haemoglobins derived from different glacial refugia in the bank vole.Proceedings. Biological sciences · 2014Article
- Hemoglobin function and allosteric regulation in semi-fossorial rodents (family Sciuridae) with different altitudinal ranges.The Journal of experimental biology · 2013Article
- Phenotypic plasticity in blood-oxygen transport in highland and lowland deer mice.The Journal of experimental biology · 2013Article
- Deer mouse hemoglobin exhibits a lowered oxygen affinity owing to mobility of the E helix.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Antioxidant functions for the hemoglobin β93 cysteine residue in erythrocytes and in the vascular compartment in vivo.Free radical biology & medicine · 2013Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
House mice (genus Mus) harbor extensive allelic variation at two tandemly duplicated genes that encode the β-chain subunits of adult hemoglobin (Hb). Alternative haplotypes differ in the level of sequence divergence between the two β-globin gene duplicates: the Hbb(d) and Hbb(p) haplotypes harbor two structurally distinct β-globin genes, whereas the Hbb(s) haplotype harbors two β-globin duplicates that are identical in sequence. One especially salient difference between the s-type Hbs relative to the d- and p-type Hbs relates to the number of reactive β-chain cysteine residues. In addition to the highly conserved cysteine residue at β93, the d- and p-type Hbs contain an additional reactive cysteine residue at β13. To assess the functional consequences of allelic variation in β-globin cysteine content, we measured O(2)-binding properties and H(2)O(2)-induced oxidation rates of mono- and dicysteinyl β-Hbs from 4 different inbred strains of mice: C57BL/6J, BALB/cJ, MSM/Ms, and CAROLI/EiJ. The experiments revealed that purified Hbs from the various mouse strains did not exhibit substantial variation in O(2)-binding properties, but s-type Hb (which contains a single reactive β-chain cysteine residue) was far more readily oxidized to Fe(3+) metHb by H(2)O(2) than other mouse Hbs that contain two reactive β-chain cysteine residues. These results suggest that the possession of an additional reactive cysteine residue may protect against metHb formation under oxidizing conditions. The allelic differences in β-globin cysteine content could affect aspects of redox signaling and oxidative/nitrosative stress responses that are mediated by Hb-S-nitrosylation and Hb-S-glutathionylation pathways.
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