title: A ubiquitously expressed human hexacoordinate hemoglobin.
abstract: We have identified a new human hemoglobin that we call histoglobin because it is expressed in a wide array of tissues. Histoglobin shares less than 30% identity with the other human hemoglobins, and the gene contains an intron in an unprecedented location. Spectroscopic and kinetic experiments with recombinant human histoglobin indicate that it is a hexacoordinate hemoglobin with significantly different ligand binding characteristics than the other human hexacoordinate hemoglobin, neuroglobin. In contrast to the very high oxygen affinities displayed by most hexacoordinate hemoglobins, the biophysical characteristics of histoglobin indicate that it could facilitate oxygen transport. The discovery of histoglobin demonstrates that humans, like plants, differentially express multiple hexacoordinate hemoglobins.
authors.affiliation: Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011, USA.
authors.forename: James T
authors.initials: JT
authors.lastname: Trent
authors.forename: Mark S
authors.initials: MS
authors.lastname: Hargrove
mesh_terms: D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D000078842:Cytoglobin; D018076:DNA, Complementary / Q000378:metabolism; D005091:Exons; D005914:Globins; D006418:Heme / Q000737:chemistry; D006454:Hemoglobins / Q000096:biosynthesis* / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D008024:Ligands; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D011485:Protein Binding; D012313:RNA / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D013053:Spectrophotometry; D013997:Time Factors; D014018:Tissue Distribution
chemical_list: D000078842:Cytoglobin; D018076:DNA, Complementary; D006454:Hemoglobins; D008024:Ligands; D011994:Recombinant Proteins; D006418:Heme; D012313:RNA; D005914:Globins