Exploring the Fe(III) binding sites of human serum transferrin with EPR at 275 GHz
Gespeichert in:
Verfasser / Beitragende:
[Guinevere Mathies, Peter Gast, N. Chasteen, Ashley Luck, Anne Mason, Edgar Groenen]
Ort, Verlag, Jahr:
2015
Enthalten in:
JBIC Journal of Biological Inorganic Chemistry, 20/3(2015-04-01), 487-496
Format:
Artikel (online)
Online Zugang:
| LEADER | caa a22 4500 | ||
|---|---|---|---|
| 001 | 605507341 | ||
| 003 | CHVBK | ||
| 005 | 20210128100631.0 | ||
| 007 | cr unu---uuuuu | ||
| 008 | 210128e20150401xx s 000 0 eng | ||
| 024 | 7 | 0 | |a 10.1007/s00775-014-1229-z |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00775-014-1229-z | ||
| 245 | 0 | 0 | |a Exploring the Fe(III) binding sites of human serum transferrin with EPR at 275 GHz |h [Elektronische Daten] |c [Guinevere Mathies, Peter Gast, N. Chasteen, Ashley Luck, Anne Mason, Edgar Groenen] |
| 520 | 3 | |a We report 275 GHz EPR spectra of human serum transferrin. At this high microwave frequency the zero-field splitting between the magnetic sublevels of the high-spin $$\text{Fe}^{3+}$$ Fe 3 + sites can be accurately determined. We find the zero-field splitting to be a sensitive probe of the structure of the transferrin iron-binding sites. Signals arising from iron bound to the transferrin N-lobe can clearly be distinguished from signals from iron bound to the C-lobe. Moreover, our spectra show that the structure of the iron site in the N-lobe is influenced by the presence and conformation of the C-lobe. The spectra of a series of N-lobe mutants altering the second-shell interaction of Arg124 with the synergistic anion carbonate reflect conformational changes induced at the iron site. | |
| 540 | |a SBIC, 2014 | ||
| 690 | 7 | |a High-frequency EPR |2 nationallicence | |
| 690 | 7 | |a High-spin $$\text{Fe}^{3+}$$ Fe 3 + |2 nationallicence | |
| 690 | 7 | |a Human serum transferrin |2 nationallicence | |
| 690 | 7 | |a Zero-field splitting |2 nationallicence | |
| 700 | 1 | |a Mathies |D Guinevere |u Department of Physics, Huygens-Kamerlingh Onnes Laboratory, Leiden University, Leiden, The Netherlands |4 aut | |
| 700 | 1 | |a Gast |D Peter |u Department of Physics, Huygens-Kamerlingh Onnes Laboratory, Leiden University, Leiden, The Netherlands |4 aut | |
| 700 | 1 | |a Chasteen |D N. |u Department of Chemistry, Parsons Hall, University of New Hampshire, 03824, Durham, NH, USA |4 aut | |
| 700 | 1 | |a Luck |D Ashley |u Department of Biochemistry, University of Vermont College of Medicine, 05405, Burlington, VT, USA |4 aut | |
| 700 | 1 | |a Mason |D Anne |u Department of Biochemistry, University of Vermont College of Medicine, 05405, Burlington, VT, USA |4 aut | |
| 700 | 1 | |a Groenen |D Edgar |u Department of Physics, Huygens-Kamerlingh Onnes Laboratory, Leiden University, Leiden, The Netherlands |4 aut | |
| 773 | 0 | |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/3(2015-04-01), 487-496 |x 0949-8257 |q 20:3<487 |1 2015 |2 20 |o 775 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00775-014-1229-z |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/s00775-014-1229-z |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Mathies |D Guinevere |u Department of Physics, Huygens-Kamerlingh Onnes Laboratory, Leiden University, Leiden, The Netherlands |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Gast |D Peter |u Department of Physics, Huygens-Kamerlingh Onnes Laboratory, Leiden University, Leiden, The Netherlands |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Chasteen |D N. |u Department of Chemistry, Parsons Hall, University of New Hampshire, 03824, Durham, NH, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Luck |D Ashley |u Department of Biochemistry, University of Vermont College of Medicine, 05405, Burlington, VT, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Mason |D Anne |u Department of Biochemistry, University of Vermont College of Medicine, 05405, Burlington, VT, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Groenen |D Edgar |u Department of Physics, Huygens-Kamerlingh Onnes Laboratory, Leiden University, Leiden, The Netherlands |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/3(2015-04-01), 487-496 |x 0949-8257 |q 20:3<487 |1 2015 |2 20 |o 775 | ||