Oxido-reduction is not the only mechanism allowing ions to traverse the ferritin protein shell

Biochimica et Biophysica Acta - General Subjects

Volumn 1800, Issue 8, 2010, Pages 745-759

  Watt, Richard K ^a   Hilton, Robert J ^a   Graff, D Matthew ^a  

^a Brigham Young University   (United States)

Author keywords

Anion transport; Bacterioferritin; Ferritin iron release; Gated pores; Long range electron transfer; Oxido reduction

Indexed keywords

ANION; CHELATING AGENT; CHLORIDE ION; FERRITIN; HYDROXIDE; METALLOCHAPERONE; PHOSPHATE;

CHELATION; CYTOSOL; EQUILIBRIUM CONSTANT; IN VITRO STUDY; IN VIVO STUDY; IRON KINETICS; LYSOSOME; NANOPORE; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; REVIEW;

ANIMALS; BIOLOGICAL TRANSPORT; CATALYTIC DOMAIN; FERRITINS; HUMANS; IONS; IRON; MODELS, BIOLOGICAL; MODELS, MOLECULAR; OXIDATION-REDUCTION; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS;

EID: 77953807901     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2010.03.001     Document Type: Review

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