Reduction of mammalian ferritin.

نویسندگان

  • G D Watt
  • R B Frankel
  • G C Papaefthymiou
چکیده

Mammalian ferritin from horse spleen undergoes an electrochemical or chemical reduction reaction in which each iron atom present is reduced by one electron (2300 electrons per ferritin molecule containing 2300 Fe3+ ions). Midpoint potentials of -190 mV, -310 mV, and -416 mV were determined at pH 7.0, 8.0, and 9.0. This variation of potential with pH indicates that approximately 2 H+ are transferred to the core for each Fe3+ reduced to Fe2+. Mössbauer measurements of partially reduced ferritin give spectra that consist of a ferric quadrupole doublet with a superposed ferrous quadrupole doublet. The relative intensities of these doublets are consistent with the electrochemically determined degree of reduction.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Redox reactivity of bacterial and mammalian ferritin: is reductant entry into the ferritin interior a necessary step for iron release?

Both mammalian and bacterial ferritin undergo rapid reaction with small-molecule reductants, in the absence of Fe2+ chelators, to form ferritins with reduced (Fe2+) mineral cores. Large, low-potential reductants (flavoproteins and ferredoxins) similarly react anaerobically with both ferritin types to quantitatively produce Fe2+ in the ferritin cores. The oxidation of Fe2+ ferritin by large prot...

متن کامل

The effect of eight weeks of concurrent exercise on NT-proBNP and ferritin serum levels of Beta Thalassemia Major patients

Introduction: Nowadays one of the most important problems of Thalassemia major patients is the additional load of iron and hemosiderosis, the most important consequence of which is deposited iron in myocardial tissue and the incidence of cardiomyopathy caused by hemochromatosis. The aim of this study was to determine the effect of concurrent (resistance-endurance) exercise on NT-pro BNP and...

متن کامل

BINDING OF Fe2+ BY MAMMALIAN FERRITIN

An average of 140 Fe 2 + ions bind to mammalian ferritin that has an average core content of 1876 Fe+ ions per molecule. The Fe2+ ions enter the protein interior and exchange electrons with the core Fe+ ions. A non-homogeneous model for the iron-eontaining core of ferritin is proposed.

متن کامل

Ferroportin-mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome.

Ferritin is a cytosolic molecule comprised of subunits that self-assemble into a nanocage capable of containing up to 4500 iron atoms. Iron stored within ferritin can be mobilized for use within cells or exported from cells. Expression of ferroportin (Fpn) results in export of cytosolic iron and ferritin degradation. Fpn-mediated iron loss from ferritin occurs in the cytosol and precedes ferrit...

متن کامل

MOSSBAUER SPECIROSCOPY OF Fe 2+ BINDING TO APO AND HOLO MAMMALIAN FERRITIN

The anaerobic binding of Fe 2+ to apo and holo Mammalian ferritin has been studied in the pH range from 6.0 to 10.0. Mossbauer spectroscopy of samples in which the added Fe 2+ is enriched in Fe-57 shows that the Fe 2+ ions bind to the ferritin core and exchange electrons with Fe 3+ ions in the core.

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Proceedings of the National Academy of Sciences of the United States of America

دوره 82 11  شماره 

صفحات  -

تاریخ انتشار 1985