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Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen.
J T Trent1, R A Watts, M S Hargrove
1Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011, USA.
The Journal of Biological Chemistry
|June 29, 2001
Summary
Neuroglobin, a brain-expressed hemoglobin, is the first vertebrate hexacoordinate hemoglobin. Its oxygen affinity suggests it does not function in traditional oxygen storage or transport.
Area of Science:
- Biochemistry
- Neuroscience
- Molecular Biology
Background:
- Neuroglobin is a recently identified mammalian hemoglobin primarily found in the brain.
- It exhibits low sequence identity (<25%) with other vertebrate globins and related invertebrate proteins.
Purpose of the Study:
- To characterize the biochemical and functional properties of human neuroglobin.
- To investigate the implications of its unique hexacoordinate structure and oxygen binding affinity.
Main Methods:
- Spectroscopic analysis of recombinant human neuroglobin.
- Kinetic experiments to determine oxygen binding characteristics.
Main Results:
- Human neuroglobin is identified as the first hexacoordinate hemoglobin in vertebrates.
- It shares structural similarities with plant and bacterial hexacoordinate hemoglobins.
- Neuroglobin's determined oxygen affinity is too low for traditional oxygen storage and transport roles.
Conclusions:
- Neuroglobin's hexacoordination and low oxygen affinity suggest novel physiological functions beyond oxygen transport.
- Further research is needed to elucidate the specific roles of neuroglobin in the brain.