| Autor: |
Trent JT 3rd; Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011, USA., Watts RA, Hargrove MS |
| Jazyk: |
angličtina |
| Zdroj: |
The Journal of biological chemistry [J Biol Chem] 2001 Aug 10; Vol. 276 (32), pp. 30106-10. Date of Electronic Publication: 2001 Jun 27. |
| DOI: |
10.1074/jbc.C100300200 |
| Abstrakt: |
Neuroglobin is a newly discovered mammalian hemoglobin that is expressed predominately in the brain (Burmester, T., Welch, B., Reinhardt, S., and Hankeln, T. (2000) Nature 407, 520-523). Neuroglobin has less than 25% identity with other vertebrate globins and shares less than 30% identity with the annelid nerve myoglobin it most closely resembles among known hemoglobins. Spectroscopic and kinetic experiments with the recombinant protein indicate that human neuroglobin is the first example of a hexacoordinate hemoglobin in vertebrates and is similar to plant and bacterial hexacoordinate hemoglobins in several respects. The ramifications of hexacoordination and potential physiological roles are explored in light of the determination of an O(2) affinity that precludes neuroglobin from functioning in traditional O(2) storage and transport. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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