Fe2+ substrate transport through ferritin protein cage ion channels influences enzyme activity and biomineralization
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| 024 | 7 | 0 | |a 10.1007/s00775-015-1279-x |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00775-015-1279-x | ||
| 245 | 0 | 0 | |a Fe2+ substrate transport through ferritin protein cage ion channels influences enzyme activity and biomineralization |h [Elektronische Daten] |c [Rabindra Behera, Rodrigo Torres, Takehiko Tosha, Justin Bradley, Celia Goulding, Elizabeth Theil] |
| 520 | 3 | |a Ferritins, complex protein nanocages, form internal iron-oxy minerals (Fe2O3·H2O), by moving cytoplasmic Fe2+ through intracage ion channels to cage-embedded enzyme (2Fe2+/O2 oxidoreductase) sites where ferritin biomineralization is initiated. The products of ferritin enzyme activity are diferric oxy complexes that are mineral precursors. Conserved, carboxylate amino acid side chains of D127 from each of three cage subunits project into ferritin ion channels near the interior ion channel exits and, thus, could direct Fe2+ movement to the internal enzyme sites. Ferritin D127E was designed and analyzed to probe properties of ion channel size and carboxylate crowding near the internal ion channel opening. Glu side chains are chemically equivalent to, but longer by one -CH2 than Asp, side chains. Ferritin D127E assembled into normal protein cages, but diferric peroxo formation (enzyme activity) was not observed, when measured at 650nm (DFP λ max). The caged biomineral formation, measured at 350nm in the middle of the broad, nonspecific Fe3+-O absorption band, was slower. Structural differences (protein X-ray crystallography), between ion channels in wild type and ferritin D127E, which correlate with the inhibition of ferritin D127E enzyme activity include: (1) narrower interior ion channel openings/pores; (2) increased numbers of ion channel protein-metal binding sites, and (3) a change in ion channel electrostatics due to carboxylate crowding. The contributions of ion channel size and structure to ferritin activity reflect metal ion transport in ion channels are precisely regulated both in ferritin protein nanocages and membranes of living cells. | |
| 540 | |a SBIC, 2015 | ||
| 690 | 7 | |a Ferritin |2 nationallicence | |
| 690 | 7 | |a Iron oxidation |2 nationallicence | |
| 690 | 7 | |a Ion channels |2 nationallicence | |
| 690 | 7 | |a Crystal structure |2 nationallicence | |
| 690 | 7 | |a Electrostatics |2 nationallicence | |
| 690 | 7 | |a Di-iron center |2 nationallicence | |
| 690 | 7 | |a Diferric peroxo |2 nationallicence | |
| 690 | 7 | |a Caged iron-oxy biomineral |2 nationallicence | |
| 690 | 7 | |a Oxidoreductase enzyme reactivity |2 nationallicence | |
| 690 | 7 | |a DFP : Diferric peroxo |2 nationallicence | |
| 690 | 7 | |a WT : Wild type |2 nationallicence | |
| 690 | 7 | |a di-Fe2+/O2 center : Oxidoreductase or ferroxidase center (Fox Center) |2 nationallicence | |
| 700 | 1 | |a Behera |D Rabindra |u Children's Hospital Oakland Research Institute (CHORI), 5700 Martin Luther King Jr. Way, 94609, Oakland, CA, USA |4 aut | |
| 700 | 1 | |a Torres |D Rodrigo |u Department of Molecular Biology and Biochemistry, University of California-Irvine, 92697, Irvine, CA, USA |4 aut | |
| 700 | 1 | |a Tosha |D Takehiko |u Children's Hospital Oakland Research Institute (CHORI), 5700 Martin Luther King Jr. Way, 94609, Oakland, CA, USA |4 aut | |
| 700 | 1 | |a Bradley |D Justin |u Children's Hospital Oakland Research Institute (CHORI), 5700 Martin Luther King Jr. Way, 94609, Oakland, CA, USA |4 aut | |
| 700 | 1 | |a Goulding |D Celia |u Department of Molecular Biology and Biochemistry, University of California-Irvine, 92697, Irvine, CA, USA |4 aut | |
| 700 | 1 | |a Theil |D Elizabeth |u Children's Hospital Oakland Research Institute (CHORI), 5700 Martin Luther King Jr. Way, 94609, Oakland, CA, USA |4 aut | |
| 773 | 0 | |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/6(2015-09-01), 957-969 |x 0949-8257 |q 20:6<957 |1 2015 |2 20 |o 775 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00775-015-1279-x |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a research-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00775-015-1279-x |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Behera |D Rabindra |u Children's Hospital Oakland Research Institute (CHORI), 5700 Martin Luther King Jr. Way, 94609, Oakland, CA, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Torres |D Rodrigo |u Department of Molecular Biology and Biochemistry, University of California-Irvine, 92697, Irvine, CA, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Tosha |D Takehiko |u Children's Hospital Oakland Research Institute (CHORI), 5700 Martin Luther King Jr. Way, 94609, Oakland, CA, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Bradley |D Justin |u Children's Hospital Oakland Research Institute (CHORI), 5700 Martin Luther King Jr. Way, 94609, Oakland, CA, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Goulding |D Celia |u Department of Molecular Biology and Biochemistry, University of California-Irvine, 92697, Irvine, CA, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Theil |D Elizabeth |u Children's Hospital Oakland Research Institute (CHORI), 5700 Martin Luther King Jr. Way, 94609, Oakland, CA, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/6(2015-09-01), 957-969 |x 0949-8257 |q 20:6<957 |1 2015 |2 20 |o 775 | ||