Concerted Motions Networking Pores and Distant Ferroxidase Centers Enable Bacterioferritin Function and Iron Traffic

X-ray crystallography, molecular dynamics (MD) simulations, and biochemistry were utilized to investigate the effect of introducing hydrophobic interactions in the 4-fold (N148L and Q151L) and B-pores (D34F) of Pseudomonas aeruginosa bacterioferritin B (BfrB) on BfrB function. The structures show on...

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Veröffentlicht in:	Biochemistry (Easton) 2015-03, Vol.54 (8), p.1611-1627
Hauptverfasser:	Yao, Huili, Rui, Huan, Kumar, Ritesh, Eshelman, Kate, Lovell, Scott, Battaile, Kevin P, Im, Wonpil, Rivera, Mario
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution Bacterial Outer Membrane Proteins - chemistry Bacterial Outer Membrane Proteins - genetics Bacterial Outer Membrane Proteins - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Catalytic Domain Ceruloplasmin - chemistry Ceruloplasmin - genetics Ceruloplasmin - metabolism Crystallography, X-Ray Cytochrome b Group - chemistry Cytochrome b Group - genetics Cytochrome b Group - metabolism Ferritins - chemistry Ferritins - genetics Ferritins - metabolism Hydrophobic and Hydrophilic Interactions Iron Models, Molecular Mutation, Missense Oxidation-Reduction Protein Folding Pseudomonas aeruginosa - chemistry Pseudomonas aeruginosa - genetics Pseudomonas aeruginosa - metabolism
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