Structure and reactivity of hexacoordinate hemoglobins

• Published in: Biophysical chemistry 2010-11, Vol.152 (1), p.1-14
• Main Authors: Kakar, Smita, Hoffman, Federico G., Storz, Jay F., Fabian, Marian, Hargrove, Mark S.
• Format: Article
• Language: English
• Subjects: Animals; Evolution; Globins - chemistry; Globins - classification; Globins - metabolism; Hemoglobins - chemistry; Hemoglobins - classification; Hemoglobins - metabolism; Hexacoordinate hemoglobin; Histidine - chemistry; Kinetics; Ligand binding; Nerve Tissue Proteins - chemistry; Nerve Tissue Proteins - metabolism; Neuroglobin; Plant hemoglobin; Protein Structure, Tertiary; Structure
• ISSN: 0301-4622; 1873-4200
• DOI: 10.1016/j.bpc.2010.08.008

The heme prosthetic group in hemoglobins is most often attached to the globin through coordination of either one or two histidine side chains. Those proteins with one histidine coordinating the heme iron are called “pentacoordinate” hemoglobins, a group represented by red blood cell hemoglobin and most other oxygen transporters. Those with two histidines are called “hexacoordinate hemoglobins”, which have broad representation among eukaryotes. Coordination of the second histidine in hexacoordinate Hbs is reversible, allowing for binding of exogenous ligands like oxygen, carbon monoxide, and nitric oxide. Research over the past several years has produced a fairly detailed picture of the structure and biochemistry of hexacoordinate hemoglobins from several species including neuroglobin and cytoglobin in animals, and the nonsymbiotic hemoglobins in plants. However, a clear understanding of the physiological functions of these proteins remains an elusive goal. [Display omitted] ►A review of hexacoordinate hemoglobin structure and function. ►The phylogeny of hexacoordinate hemoglobins. ►A review of ligand binding to hexacoordinate hemoglobins.