ArticleBiochemistry2008
Interfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Hemoglobin-based oxygen carriers: evolution, translational applications and clinical considerations.Frontiers in medicine · 2026Review
- Global Environmental Factors Impact the Evolution of Adult Hemoglobins in Squamata Reptiles (Lizards and Snakes) and Terrestrial Turtles.Genome biology and evolution · 2025Article
- Precise Engineering and Efficient Biosynthesis of Robust and High-Activity Human Haemoglobin for Artificial Oxygen Carriers.Microbial biotechnology · 2025Article
- Hemoglobin Variants as Targets for Stabilizing Drugs.Molecules (Basel, Switzerland) · 2025Review
- Current Challenges in the Development of Acellular Hemoglobin Oxygen Carriers by Protein Engineering.Shock (Augusta, Ga.) · 2019Review
- New look at hemoglobin allostery.Chemical reviews · 2015Review
- Repeated elevational transitions in hemoglobin function during the evolution of Andean hummingbirds.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Development of recombinant hemoglobin-based oxygen carriers.Antioxidants & redox signaling · 2013Review
- A biochemical--biophysical study of hemoglobins from woolly mammoth, Asian elephant, and humans.Biochemistry · 2011Article
- Modulating distal cavities in the α and β subunits of human HbA reveals the primary ligand migration pathway.Biochemistry · 2011Article
- WAXS studies of the structural diversity of hemoglobin in solution.Journal of molecular biology · 2011Article
- An investigation of the distal histidyl hydrogen bonds in oxyhemoglobin: effects of temperature, pH, and inositol hexaphosphate.Biochemistry · 2010Article
- Distal histidine stabilizes bound O2 and acts as a gate for ligand entry in both subunits of adult human hemoglobin.The Journal of biological chemistry · 2010Article
- Recombinant hemoglobin II from Lucina pectinata: a large-scale method for hemeprotein expression in E. coli.The protein journal · 2010Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Protein engineering strategies seek to develop a hemoglobin-based oxygen carrier with optimized functional properties, including (i) an appropriate O 2 affinity, (ii) high cooperativity, (iii) limited NO reactivity, and (iv) a diminished rate of auto-oxidation. The mutations alphaL29F, alphaL29W, alphaV96W and betaN108K individually impart some of these traits and in combinations produce hemoglobin molecules with interesting ligand-binding and allosteric properties. Studies of the ligand-binding properties and solution structures of single and multiple mutants have been performed. The aromatic side chains placed in the distal-heme pocket environment affect the intrinsic ligand-binding properties of the mutated subunit itself, beyond what can be explained by allostery, and these changes are accompanied by local structural perturbations. In contrast, hemoglobins with mutations in the alpha 1beta 1 and alpha 1beta 2 interfaces display functional properties of both "R"- and "T"-state tetramers because the equilibrium between quaternary states is altered. These mutations are accompanied by global structural perturbations, suggesting an indirect, allostery-driven cause for their effects. Combinations of the distal-heme pocket and interfacial mutations exhibit additive effects in both structural and functional properties, contribute to our understanding of allostery, and advance protein-engineering methods for manipulating the O 2 binding properties of the hemoglobin molecule.
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