A Membrane-bound Hemoglobin from Gills of the Green Shore Crab Carcinus maenas
| Autor: | Michael C. Marden, Miriam Blank, Thorsten Burmester, Laurent Kiger, Beyhan Ertas |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Gills
Gill Brachyura medicine.medical_treatment Molecular Sequence Data Biochemistry Hemoglobins Hemolymph medicine Animals Tissue Distribution Carcinus maenas Molecular Biology biology Ecology fungi Oxygen transport Membrane Proteins Hemocyanin Cell Biology biology.organism_classification Oxygen Respiratory protein Hemoglobin Oxygen binding |
| Zdroj: | Journal of Biological Chemistry. 286:3185-3193 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m110.160341 |
| Popis: | Most hemoglobins serve for the transport or storage of O(2). Although hemoglobins are widespread in "entomostracan" Crustacea, malacostracans harbor the copper-containing hemocyanin in their hemolymph. Usually, only one type of respiratory protein occurs within a single species. Here, we report the identification of a hemoglobin of the shore crab Carcinus maenas (Malacostraca, Brachyura). In contrast to the dodecameric hemocyanin of this species, C. maenas hemoglobin does not reside in the hemolymph but is restricted to the gills. Immunofluorescence studies and cell fractioning showed that C. maenas hemoglobin resides in the membrane of the chief cells of the gill. To the best of our knowledge, this is the first time that a membrane-bound hemoglobin has been identified in eukaryotes. Bioinformatic evaluation suggests that C. maenas hemoglobin is anchored in the membrane by N-myristoylation. Recombinant C. maenas hemoglobin has a hexacoordinate binding scheme at the Fe(2+) and an oxygen affinity of P(50) = 0.5 Torr. A rapid autoxidation rate precludes a function as oxygen carrier. We rather speculate that, analogous to prokaryotic membrane-globins, C. maenas hemoglobin carries out enzymatic functions to protect the lipids in cell membrane from reactive oxygen species. Sequence comparisons and phylogenetic studies suggested that the ancestral arthropod hemoglobin was most likely an N-myristoylated protein that did not have an O(2) supply function. True respiratory hemoglobins of arthropods, however, evolved independently in chironomid midges and branchiopod crustaceans. |
| Databáze: | OpenAIRE |
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