Related ArticlesIron uptake by ferritin: NMR relaxometry studies at low iron loads.
J Inorg Biochem. 1998 Sep;71(3-4):153-7
Authors: Vymazal J, Brooks RA, Bulte JW, Gordon D, Aisen P
Twenty ferritin samples were prepared at pH 6.5 with average loadings of 0-89 Fe atoms per molecule. Nuclear magnetic relaxation times T1 and T2 were measured at 3 degrees C, 23 degrees C, and at 37 degrees C and at field strength from 0.025 to 1.5 T. The field dependence, temperature dependence, and approximate equality of T1 and T2 at low fields all suggest that nuclear magnetic relaxation in this range is caused primarily by solitary Fe3+ ions. The relaxivity (relaxation rate per mM ferritin) increases quickly with initial iron loading, reaches a peak at 13-14 Fe atoms per molecule, and then declines. This provides supportive evidence for the formation of antiferromagnetically-coupled clusters during early stages in iron loading; the failure to see a similar peak in an earlier study may be related to the nonphysiological pH that was used. Above 50 atoms per molecule, the relaxivity remains approximately constant, except that 1/T2 at high fields increases slightly, consistent with early core growth. The residual ionic relaxivity in this region is consistent with about three solitary Fe3+ ions remaining on the protein shell, indicating that spin cancellation is not complete. A similar value is obtained by extrapolating relaxation data at high loadings (up to 3000 Fe atoms per molecule), suggesting that these uncoupled spins persist on the protein shell even after an appreciable core has been built.
[NMR paper] Two-iron rubredoxin of Pseudomonas oleovorans: production, stability and characteriza
Two-iron rubredoxin of Pseudomonas oleovorans: production, stability and characterization of the individual iron-binding domains by optical, CD and NMR spectroscopies.
Related Articles Two-iron rubredoxin of Pseudomonas oleovorans: production, stability and characterization of the individual iron-binding domains by optical, CD and NMR spectroscopies.
Biochem J. 2001 Feb 15;354(Pt 1):89-98
Authors: Perry A, Lian LY, Scrutton NS
A minigene encoding the C-terminal domain of the 2Fe rubredoxin of Pseudomonas oleovorans was created from the...
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[NMR paper] Amino acid-specific isotopic labeling and active site NMR studies of iron(II)- and ir
Amino acid-specific isotopic labeling and active site NMR studies of iron(II)- and iron(III)-superoxide dismutase from Escherichia coli.
Related Articles Amino acid-specific isotopic labeling and active site NMR studies of iron(II)- and iron(III)-superoxide dismutase from Escherichia coli.
J Biomol NMR. 2000 Aug;17(4):311-22
Authors: Sorkin DL, Miller AF
We have developed and employed multiple amino acid-specific isotopic labeling schemes to obtain definitive assignments for active site 1H NMR resonances of iron(II)- and iron(III)-superoxide...
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[NMR paper] Exploration of the structural environment of the iron-sulfur cluster in putidaredoxin
Exploration of the structural environment of the iron-sulfur cluster in putidaredoxin by nitrogen-15 NMR spectroscopy of selectively labeled cysteine residues.
Related Articles Exploration of the structural environment of the iron-sulfur cluster in putidaredoxin by nitrogen-15 NMR spectroscopy of selectively labeled cysteine residues.
Biochem Biophys Res Commun. 1998 Aug 28;249(3):773-80
Authors: Sari N, Holden MJ, Mayhew MP, Vilker VL, Coxon B
Putidaredoxin is a di-iron protein whose paramagnetic region is not well characterized by 1H...
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[NMR paper] Proton NMR investigation of the [4Fe--4S]1+ cluster environment of nitrogenase iron p
Proton NMR investigation of the 1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes.
Related Articles Proton NMR investigation of the 1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes.
Biochemistry. 1995 Dec 5;34(48):15646-53
Authors: Lanzilotta WN, Holz RC, Seefeldt LC
This work presents the complete assignment of the isotropically shifted 1H NMR resonances of Azotobacter vinelandii...
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[NMR paper] 1H NMR investigation of the electronic and molecular structure of the four-iron clust
1H NMR investigation of the electronic and molecular structure of the four-iron cluster ferredoxin from the hyperthermophile Pyrococcus furiosus. Identification of Asp 14 as a cluster ligand in each of the four redox states.
Related Articles 1H NMR investigation of the electronic and molecular structure of the four-iron cluster ferredoxin from the hyperthermophile Pyrococcus furiosus. Identification of Asp 14 as a cluster ligand in each of the four redox states.
Biochemistry. 1995 Sep 12;34(36):11373-84
Authors: Calzolai L, Gorst CM, Zhao ZH, Teng Q,...
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[NMR paper] The importance of a single G in the hairpin loop of the iron responsive element (IRE)
The importance of a single G in the hairpin loop of the iron responsive element (IRE) in ferritin mRNA for structure: an NMR spectroscopy study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles The importance of a single G in the hairpin loop of the iron responsive element (IRE) in ferritin mRNA for structure: an NMR spectroscopy study.
Nucleic Acids Res. 1995 Jan 11;23(1):146-53
Authors: Sierzputowska-Gracz H, McKenzie RA, Theil EC
Noncoding sequences...
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[NMR paper] NMR studies of Azotobacter vinelandii and Pseudomonas putida seven-iron ferredoxins.
NMR studies of Azotobacter vinelandii and Pseudomonas putida seven-iron ferredoxins. Direct assignment of beta-cysteinyl carbon NMR resonances and further proton NMR assignments of cysteinyl and aromatic resonances.
Related Articles NMR studies of Azotobacter vinelandii and Pseudomonas putida seven-iron ferredoxins. Direct assignment of beta-cysteinyl carbon NMR resonances and further proton NMR assignments of cysteinyl and aromatic resonances.
J Biol Chem. 1992 Apr 25;267(12):8073-80
Authors: Cheng H, Grohmann K, Sweeney W
Ferredoxins are...
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[NMR paper] 1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nucle
1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nuclear Overhauser effect measurements.
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Biochemistry. 1990 Jun 12;29(23):5633-7
Authors: Cowan JA, Sola M
1H nuclear Overhauser effect experiments on the isotropically shifted signals of oxidized Chromatium vinosum HiPIP have been used to identify the four beta-CH2 geminal couples of the cysteine ligands. A partial assignment to...