Characterization of the hemoglobin of the backswimmer Anisops deanei (Hemiptera).
Characterization of the hemoglobin of the backswimmer Anisops deanei (Hemiptera).
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DOI:
10.1016/j.ibmb.2012.04.007
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发表时间:
2012-09
影响因子:
3.8
通讯作者:
Agnes Wawrowski;P. G. D. Matthews;E. Gleixner;L. Kiger;M. Marden;T. Hankeln;T. Burmester
中科院分区:
文献类型:
--
作者:
Agnes Wawrowski;P. G. D. Matthews;E. Gleixner;L. Kiger;M. Marden;T. Hankeln;T. Burmester
While O2-binding hemoglobin-like proteins are present in many insects, prominent amounts of hemoglobin have only been found in a few species. Backswimmers of the genera Anisops and Buenoa (Notonectidae) have high concentrations of hemoglobin in the large tracheal cells of the abdomen. Oxygen from the hemoglobin is delivered to a gas bubble and controls the buoyant density, which enables the bugs to maintain their position without swimming and to remain stationary in the mid-water zone where they hunt for prey. We have obtained the cDNA sequences of three Anisops deanei hemoglobin chains by RT-PCR and RACE techniques. The deduced amino acid sequences show an unusual insertion of a single amino acid in the conserved helix E, but this does not affect protein stability or ligand binding kinetics. Recombinant A. deanei hemoglobin has an oxygen affinity of P50= 2.4 kPa (18 torr) and reveals the presence of a dimeric fraction or two different conformations. The absorption spectra demonstrate that the Anisops hemoglobin is a typical pentacoordinate globin. Phylogenetic analyses show that the backswimmer hemoglobins evolved within Heteroptera and most likely originated from an intracellular hemoglobin with divergent function.