Structural properties of cyanobacterial hemoglobins: the unusual heme-protein cross-link of Synechocystis sp. PCC 6803 Hb and Synechococcus sp. PCC 7002 Hb
| Autor: | Juliette T. J. Lecomte, David A. Vuletich, Nancy L. Scott, Syna A. Kuriakose, B. Christie Vu, Christopher J. Falzone |
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| Rok vydání: | 2004 |
| Předmět: |
Hemichrome
Hemeprotein Cross-link Substituent General Physics and Astronomy Truncated Hemoglobins macromolecular substances Cell Biology Biology Cyanobacteria chemistry.chemical_compound Hemoglobins Synechocystis sp Biochemistry chemistry Bacterial Proteins Structural Biology Helix bacteria General Materials Science Denaturation (biochemistry) Histidine |
| Zdroj: | Micron (Oxford, England : 1993). 35(1-2) |
| ISSN: | 0968-4328 |
| Popis: | The truncated hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002 ligate the heme iron with two axial histidines (HisF8 and HisE10). In addition, these two proteins are able to form a heme-protein cross-link between a vinyl substituent and a histidine at position 16 of the H helix. The product is a protein with improved resistance to thermal and acid denaturation. |
| Databáze: | OpenAIRE |
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