Characterization of the hemoglobin of the backswimmer Anisops deanei (Hemiptera)

Wawrowski, Agnes, Matthews, Philip G. D., Gleixner, Eva, Kiger, Laurent, Marden, Michael C., Hankeln, Thomas and Burmester, Thorsten (2012) Characterization of the hemoglobin of the backswimmer Anisops deanei (Hemiptera). Insect Biochemistry and Molecular Biology, 42 9: 603-609. doi:10.1016/j.ibmb.2012.04.007

Author Wawrowski, Agnes
Matthews, Philip G. D.
Gleixner, Eva
Kiger, Laurent
Marden, Michael C.
Hankeln, Thomas
Burmester, Thorsten
Title Characterization of the hemoglobin of the backswimmer Anisops deanei (Hemiptera)
Formatted title
Characterization of the hemoglobin of the backswimmer Anisops deanei (Hemiptera)
Journal name Insect Biochemistry and Molecular Biology   Check publisher's open access policy
ISSN 0965-1748
Publication date 2012-09
Sub-type Article (original research)
DOI 10.1016/j.ibmb.2012.04.007
Volume 42
Issue 9
Start page 603
End page 609
Total pages 7
Place of publication Oxford, United Kingdom
Publisher Pergamon
Collection year 2013
Language eng
Formatted abstract
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.
Keyword Backswimmer
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2013 Collection
School of Biological Sciences Publications
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Created: Wed, 31 Oct 2012, 14:08:17 EST by Gail Walter on behalf of School of Biological Sciences