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Biochem. Biophys. Res. Commun. · May 2005
Preparation and characterization of a chimeric zebrafish-human neuroglobin engineered by module substitution.
- Keisuke Wakasugi and Isao Morishima.
- Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto 615-8510, Japan. kei@wakasugi.mbox.media.kyoto-u.ac.jp
- Biochem. Biophys. Res. Commun. 2005 May 6;330(2):591-7.
AbstractNeuroglobin (Ngb) is a recently discovered vertebrate heme protein that can reversibly bind oxygen that is expressed in the brain. Zebrafish and human Ngb share about 50% amino acid sequence identity. These Ngb proteins consist of four compact protein structural unit "modules" referred to as M1-M4. In the present study, we investigated the effects of module substitution on the properties of Ngb. Specifically, we prepared and characterized a chimeric ZHZZ Ngb in which the heme-binding module M2 of zebrafish Ngb was replaced by the comparable human Ngb module. Our results showed that the chimeric ZHZZ was stable and formed almost the identical heme-environmental and alpha-helical structure as the human and zebrafish Ngb proteins, suggesting that the structure of Ngb has been evolutionarily conserved.
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