期刊
BIOPHYSICAL CHEMISTRY
卷 152, 期 1-3, 页码 1-14出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bpc.2010.08.008
关键词
Hexacoordinate hemoglobin; Structure; Kinetics; Ligand binding; Evolution; Plant hemoglobin; Neuroglobin
资金
- NHLBI NIH HHS [R01 HL087216] Funding Source: Medline
- Division Of Integrative Organismal Systems
- Direct For Biological Sciences [0949931] Funding Source: National Science Foundation
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. (C) 2010 Elsevier B.V. All rights reserved.
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