title: Structural properties of cyanobacterial hemoglobins: the unusual heme-protein cross-link of Synechocystis sp. PCC 6803 Hb and Synechococcus sp. PCC 7002 Hb.
abstract: 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.
authors.affiliation: Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA. jtl1@psu.edu
authors.forename: Juliette T J
authors.initials: JT
authors.lastname: Lecomte
authors.forename: David A
authors.initials: DA
authors.lastname: Vuletich
authors.forename: B Christie
authors.initials: BC
authors.lastname: Vu
authors.forename: Syna A
authors.initials: SA
authors.lastname: Kuriakose
authors.forename: Nancy L
authors.initials: NL
authors.lastname: Scott
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Falzone
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D000458:Cyanobacteria / Q000737:chemistry*; D006454:Hemoglobins / Q000737:chemistry*; D054793:Truncated Hemoglobins
chemical_list: D001426:Bacterial Proteins; D006454:Hemoglobins; D054793:Truncated Hemoglobins