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dc.contributor.authorDewilde, Sylvia  Concept link
dc.contributor.authorEbner, Bettina  Concept link
dc.contributor.authorVinck, Evi  Concept link
dc.contributor.authorGilany, Kambiz  Concept link
dc.contributor.authorHankeln, Thomas  Concept link
dc.contributor.authorBurmester, Thorsten  Concept link
dc.contributor.authorKreiling, Jill A.  Concept link
dc.contributor.authorReinisch, Carol L.  Concept link
dc.contributor.authorVanfleteren, Jacques R.  Concept link
dc.contributor.authorKiger, Laurent  Concept link
dc.contributor.authorMarden, Michael C.  Concept link
dc.contributor.authorHundahl, Christian  Concept link
dc.contributor.authorFago, Angela  Concept link
dc.contributor.authorVan Doorslaer, Sabine  Concept link
dc.contributor.authorMoens, Luc  Concept link
dc.date.accessioned2009-04-24T19:56:05Z
dc.date.available2009-04-24T19:56:05Z
dc.date.issued2005-12-13
dc.identifier.citationJournal of Biological Chemistry 281 (2006): 5364-5372en
dc.identifier.urihttps://hdl.handle.net/1912/2813
dc.descriptionAuthor Posting. © American Society for Biochemistry and Molecular Biology, 2006. This article is posted here by permission of American Society for Biochemistry and Molecular Biology for personal use, not for redistribution. The definitive version was published in Journal of Biological Chemistry 281 (2006): 5364-5372, doi:10.1074/jbc.M509486200.en
dc.description.abstractMembers of the hemoglobin (Hb) superfamily are present in nerve tissue of several vertebrate and invertebrate species. In vertebrates they display hexacoordinate heme iron atoms and are typically expressed at low levels (µM). Their function is still a matter of debate. In invertebrates they have a hexa- or pentacoordinate heme iron, are mostly expressed at high levels (mM), and have been suggested to have a myoglobin-like function. The native Hb of the surf clam, Spisula solidissima, composed of 162 amino acids, does not show specific deviations from the globin templates. UV-visible and resonance Raman spectroscopy demonstrate a hexacoordinate heme iron. Based on the sequence analogy, the histidine E7 is proposed as a sixth ligand. Kinetic and equilibrium measurements show a moderate oxygen affinity (P50 ~0.6 torr) and no cooperativity. The histidine binding affinity is 100-fold lower than in neuroglobin. Phylogenetic analysis demonstrates a clustering of the S. solidissima nerve Hb with mollusc Hbs and myoglobins, but not with the vertebrate neuroglobins. We conclude that invertebrate nerve Hbs expressed at high levels are, despite the hexacoordinate nature of their heme iron, not essentially different from other intracellular Hbs. They most likely fulfill a myoglobin-like function and enhance oxygen supply to the neuronsen
dc.description.sponsorshipThis study was supported in part by Inserm, University of Paris-XI, by European Union Grant QLG3-CT-2002-01548, the Deutsche Forschungsgemeinschaft (Ha2103/3 and Bu956/5), by the Fund for Scientific Research of Flanders Grant G.0468.03, and by the Danish Natural Science Research Council.en
dc.format.mimetypeapplication/pdf
dc.language.isoen_USen
dc.publisherAmerican Society for Biochemistry and Molecular Biologyen
dc.relation.urihttps://doi.org/10.1074/jbc.M509486200
dc.titleThe nerve hemoglobin of the bivalve mollusc Spisula solidissima : molecular cloning, ligand binding studies, and phylogenetic analysisen
dc.typeArticleen
dc.identifier.doi10.1074/jbc.M509486200


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