Journal of Biological Chemistry
Volume 277, Issue 32, 9 August 2002, Pages 29012-29017
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PROTEIN STRUCTURE AND FOLDING
Characterization of DrosophilaHemoglobin: EVIDENCE FOR HEMOGLOBIN-MEDIATED RESPIRATION IN INSECTS*

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In contrast to previous assumptions, the fruit fly Drosophila melanogaster possesses hemoglobin. This respiratory protein forms a monomer of about 17 kDa that is not exported into the hemolymph. Recombinant Drosophilahemoglobin displays a typical hexacoordinated deoxy spectrum and binds oxygen with an affinity of 0.12 torr. Four different hemoglobin transcripts have been identified, which are generated by two distinct promoters of the hemoglobin (glob1) gene but are identical in their coding regions. Putative binding sites for hypoxia-regulated transcription factors have been identified in the gene. Hemoglobin synthesis in Drosophila is mainly associated with the tracheal system and the fat body. This suggests that oxygen supply in insects may be more complex than thought previously and may depend on hemoglobin-mediated oxygen transport and storage in addition to simple diffusion.

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Published, JBC Papers in Press, June 4, 2002, DOI 10.1074/jbc.M204009200

*

This work was supported by the Deutsche Forschungsgemeinschaft (Grants Ha2103/3 and Bu956/5).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

**

A postdoctoral fellow of the Fund for Scientific Research– Flanders.

§

To whom correspondence may be addressed. E-mail: hankeln@ molgen.biologie.uni-mainz.de.

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To whom correspondence may be addressed. Tel.: 49-6131-39-24477; Fax: 49-6131-39-24652; E-mail: [email protected].