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 helix. The product is a protein with improved resistance to thermal and acid denaturation.
Lecomte
Juliette T J
JT
Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA. jtl1@psu.edu
Vuletich
David A
DA
Vu
B Christie
BC
Kuriakose
Syna A
SA
Scott
Nancy L
NL
Falzone
Christopher J
CJ
D001426:Bacterial Proteins / Q000737:chemistry*; D000458:Cyanobacteria / Q000737:chemistry*; D006454:Hemoglobins / Q000737:chemistry*; D054793:Truncated Hemoglobins
D001426:Bacterial Proteins; D006454:Hemoglobins; D054793:Truncated Hemoglobins