Crystallization of bacterioferritin fromBlastochloris viridis

Structural Characterization of Bacterioferritin from Blastochloris viridis

Iron storage and elimination of toxic ferrous iron are the responsibility of bacterioferritins in bacterial species. Bacterioferritins are capable of oxidizing iron using molecular oxygen and import iron ions into the large central cavity of the protein, where they are stored in a mineralized form. We isolated, crystallized bacterioferritin from the microaerophilic/anaerobic, purple non-sulfur ...

Biochemistry in Bacterioferritin

Chemosensory response in stunted prairie rattlesnakes Crotalus viridis viridis

Rattlesnakes use chemical stimuli in ambush site selection and for relocation of envenomated prey through strike-induced chemosensory searching. Shifts in responsiveness to prey chemicals have been documented in many snakes, and often correlate with prey commonly taken as snakes increase in age and size as well as geographical locations of the species. For instance, neonate rattlesnakes that pr...

ucture of the bacterioferritin from Azotobacter vinelandii

The crystal structure of the bacterioferritin from Azotobacter vinelandii has been determined at 2.6 A resolution. Both the low occupancy of one iron ion in the dinuclear iron center and the deviation of its adjacent residue His130 from the center suggest migration of the iron ion from the dinuclear iron site to the inner nucleation site. The concerted movement of His130 and Glu47 may admit a d...

Structural heterogeneity of Pseudomonas aeruginosa bacterioferritin.

The subunit composition, amino acid sequence and haem-binding characteristics of bacterioferritin (BFR) from Pseudomonas aeruginosa have been studied. Unlike other BFRs, P. aeruginosa BFR was found to contain two subunit types, designated alpha and beta, which differed considerably in their amino acid sequences. The N-terminal 69 and 55 amino acids of the alpha and beta subunits respectively we...