Abstract
Hemoglobin is the respiratory protein of many arthropods, enhancing the oxygen transport capacity of the hemolymph. One example, that has been subject of extensive studies, is the hemoglobin of the crustacean genus Daphnia. Here the characteristics of this oxygen binding protein are reviewed. The genetic structure is the result of repeated duplication events in the evolution, leading to a variety of di-domain isoforms. Adjustments to environmental changes thus result from differential expression of these paralogs. The biochemical properties, including spectral characteristics, concentration ranges, molecular mass of monomers and native oligomers, are compared. Structural differences between isoforms can be correlated to functional properties of oxygen binding characteristics. The mechanism of hemoglobin induction via hypoxia-inducible factor 1 allows the response to altered oxygen and temperature conditions. Changes of the hemoglobin suite in quantity and functional quality can be linked to their benefits for the animals’ physiological performance. However, there is a large inter- and intra-specific variability of this induction potential. The consequences of altered hemoglobin characteristics for the animals’ success within their habitat are discussed.
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Zeis, B. (2020). Hemoglobin in Arthropods—Daphnia as a Model. In: Hoeger, U., Harris, J. (eds) Vertebrate and Invertebrate Respiratory Proteins, Lipoproteins and other Body Fluid Proteins. Subcellular Biochemistry, vol 94. Springer, Cham. https://doi.org/10.1007/978-3-030-41769-7_6
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