Structural properties of cyanobacterial hemoglobins: the unusual heme-protein cross-link of Synechocystis sp. PCC 6803 Hb and Synechococcus sp. PCC 7002 Hb

Structural properties of cyanobacterial hemoglobins: the unusual heme-protein cross-link of Synechocystis sp. PCC 6803 Hb and Synechococcus sp. PCC 7002 Hb

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 h...

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Veröffentlicht in:Micron (Oxford, England : 1993) England : 1993), 2004, Vol.35 (1), p.71-72
Hauptverfasser: Lecomte, Juliette T.J, Vuletich, David A, Vu, B.Christie, Kuriakose, Syna A, Scott, Nancy L, Falzone, Christopher J
Format: Artikel
Sprache:eng
Schlagworte:
Bacterial Proteins - chemistry
Covalent attachment
Cyanobacteria - chemistry
Cyanoglobin
Hemichrome
Hemoglobins - chemistry
Nuclear magnetic resonance
Paramagnetic complex
Truncated hemoglobin
Truncated Hemoglobins
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Zusammenfassung: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.
ISSN:0968-4328
1878-4291
DOI:10.1016/j.micron.2003.10.020