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Expression and in silico structural analysis of a rice (Oryza sativa) hemoglobin 5

Garrocho-Villegas, V., Bustos-Rivera, G., Gough, J., Vinogradov, S.N., Arredondo-Peter, R., Expression and in silico structural analysis of a rice (Oryza sativa) hemoglobin 5. Plant Physiol. Biochem., xx. ISSN 0981-9428, pp. 1–5. May 2008. PDF, 548 Kbytes.

Abstract

This work reports the analysis of an additional hemoglobin (hb) gene copy, hb5, in the genome of rice. The amino acid sequence of Hb5 differs from the previously determined rice Hbs 1a??4 in missing 11 residues in helix E. Transcripts of hb5 were found to be ubiquitous in rice organs, and hormone- and stress-response promoters exist upstream of the rice hb5 gene. Furthermore, the modeled structure of Hb5 based on the known crystal structure of rice Hb1 is unusual in that the putative distal His is distant from the heme Fe. This observation suggests that Hb5 binds and releases O2 easily and thus that it functions as an O2-carrier or in some aspects of the O2 metabolism.

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