Academic Journal

Iron entry route in horse spleen apoferritin ; Involvement of the three‐fold channels as probed by selective reaction of cysteine‐126 with the spin label 4‐maleimido‐tempo

التفاصيل البيبلوغرافية
العنوان: Iron entry route in horse spleen apoferritin ; Involvement of the three‐fold channels as probed by selective reaction of cysteine‐126 with the spin label 4‐maleimido‐tempo
المؤلفون: Desideri, A., Stefanini, S., Polizio, F., Petruzzelli, R., Chiancone, E.
المصدر: FEBS Letters ; volume 287, issue 1-2, page 10-14 ; ISSN 0014-5793 1873-3468
بيانات النشر: Wiley
سنة النشر: 1991
المجموعة: Wiley Online Library (Open Access Articles via Crossref)
الوصف: Apoferritin has been selectively labeled with a maleimide nitroxide derivative at Cys‐126, located in the hydrophilic 3‐fold channels. Titration of this derivative with Fe(II), which gives rise to the initial Fe(III)‐apoferritin complex, produces, at low metal‐to‐protein ratios, a decrease of the intensity of the label EPR signal due to the occurrence of a magnetic dipolar interaction. A label‐metal distance ranging between 8–12 Å can be estimated from titrations performed with VO(IV), which is known to bind in the 3‐fold channels, and likewise produces a decrease in the label EPR signal. The present findings indicate that iron binds in the hydrophilic channels in its higher oxidation slate and that these channels represent the metal entry route at least at low metal‐to‐protein ratios.
نوع الوثيقة: article in journal/newspaper
اللغة: English
DOI: 10.1016/0014-5793(91)80004-m
DOI: 10.1016/0014-5793%2891%2980004-M
الاتاحة: http://dx.doi.org/10.1016/0014-5793(91)80004-m
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2F0014-5793%2891%2980004-M
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2F0014-5793(91)80004-M
https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2891%2980004-M
Rights: http://onlinelibrary.wiley.com/termsAndConditions#vor
رقم الانضمام: edsbas.4E0B76EF
قاعدة البيانات: BASE
الوصف
DOI:10.1016/0014-5793(91)80004-m