Identification of citrate as the albumin-bound inhibitor of the ferroxidase activity of ceruloplasmin

1983 ◽  
Vol 5 (2) ◽  
pp. 81-90 ◽  
Author(s):  
Jerzy Witwicki ◽  
Mankulathu V. Chidambaram ◽  
Earl Frieden
Keyword(s):  
Ferroxidase Activity

scholarly journals Ferroxidase activity of ferritin: effects of pH, buffer and Fe(II) and Fe(III) concentrations on Fe(II) autoxidation and ferroxidation

1999 ◽  
Vol 338 (3) ◽  
pp. 615-618 ◽  
Author(s):  
Xiaoke YANG ◽  
N. Dennis CHASTEEN
Keyword(s):  
Ph Control ◽  
Alternative Mechanism ◽  
Experimental Conditions ◽  
Iron Storage ◽  
Ferroxidase Activity ◽  
Effects Of Ph ◽  
Ph Stat ◽  
Ph Buffer ◽  
Horse Spleen Ferritin

It is widely accepted that iron deposition in the iron storage protein ferritin in vitro involves Fe(II) oxidation, and that ferritin facilitates this oxidation at a ferroxidase site on the protein. However, these views have recently been questioned, with the protein ferroxidase activity instead being attributed to autoxidation from the buffer alone. Ligand exchange between another protein with ferroxidase activity and ferritin has been proposed as an alternative mechanism for iron incorporation into ferritin. In the present work, a pH stat apparatus is used to eliminate the influence of buffers on iron(II) oxidation. Here we show that the recent experiments questioning the ferroxidase activity of ferritin were flawed by inadequate pH control, that buffers actually retard rather than facilitate iron(II) oxidation, and that horse spleen ferritin has ferroxidase activity when measured under proper experimental conditions. Furthermore, high pH (7.0), a high Fe(II) concentration and the presence of Fe(III) all favour Fe(II) autoxidation in the presence or absence of ferritin.

Functional link between ferroxidase activity of ceruloplasmin and protective effect of apo-lactoferrin: studying rats kept on a silver chloride diet

BioMetals ◽  
2016 ◽  
Vol 29 (4) ◽  
pp. 691-704 ◽  
Author(s):  
Valeria A. Kostevich ◽  
Alexey V. Sokolov ◽  
Stanislav O. Kozlov ◽  
Anna Yu. Vlasenko ◽  
Nikolay N. Kolmakov ◽  
...  
Keyword(s):  
Protective Effect ◽  
Silver Chloride ◽  
Functional Link ◽  
Ferroxidase Activity

scholarly journals The ferroxidase LPR5 functions in the maintenance of phosphate homeostasis and is required for normal growth and development of rice

2020 ◽  
Vol 71 (16) ◽  
pp. 4828-4842
Author(s):  
Hao Ai ◽  
Yue Cao ◽  
Ajay Jain ◽  
Xiaowen Wang ◽  
Zhi Hu ◽  
...  
Keyword(s):  
Growth And Development ◽  
Xylem Sap ◽  
Sufficient Conditions ◽  
Normal Growth ◽  
Yield Potential ◽  
Specific Expression ◽  
Gus Reporter ◽  
Ferroxidase Activity ◽  
Vitro Analysis

Abstract Members of the Low Phosphate Root (LPR) family have been identified in rice (Oryza sativa) and expression analyses have been conducted. Here, we investigated the functions of one of the five members in rice, LPR5. qRT-PCR and promoter–GUS reporter analyses indicated that under Pi-sufficient conditions OsLPR5 was highly expressed in the roots, and specific expression occurred in the leaf collars and nodes, and its expression was increased under Pi-deficient conditions. In vitro analysis of the purified OsLPR5 protein showed that it exhibited ferroxidase activity. Overexpression of OsLPR5 triggered higher ferroxidase activity, and elevated concentrations of Fe(III) in the xylem sap and of total Fe in the roots and shoots. Transient expression of OsLPR5 in Nicotiana benthamiana provided evidence of its subcellular localization to the cell wall and endoplasmic reticulum. Knockout mutation in OsLPR5 by means of CRISPR-Cas9 resulted in adverse effects on Pi translocation, on the relative expression of Cis-NATOsPHO1;2, and on several morphological traits, including root development and yield potential. Our results indicate that ferroxidase-dependent OsLPR5 has both a broad-spectrum influence on growth and development in rice as well as affecting a subset of physiological and molecular traits that govern Pi homeostasis.

The Ferritin-Heavy-Polypeptide-Like-17 (FTHL17) gene encodes a ferritin with low stability and no ferroxidase activity and with a partial nuclear localization

2015 ◽  
Vol 1850 (6) ◽  
pp. 1267-1273 ◽  
Author(s):  
Paola Ruzzenenti ◽  
Michela Asperti ◽  
Stefania Mitola ◽  
Elisabetta Crescini ◽  
Federica Maccarinelli ◽  
...  
Keyword(s):  
Nuclear Localization ◽  
Ferroxidase Activity

scholarly journals A new method for assay of ferroxidase activity and its application to human and rabbit sera.

1984 ◽  
Vol 32 (10) ◽  
pp. 4029-4035 ◽  
Author(s):  
SHINZO TANABE ◽  
TOSHIKO SHIOIRI ◽  
KYOKO MURAKAMI ◽  
TOSHIO IMANARI
Keyword(s):  
New Method ◽  
Ferroxidase Activity

scholarly journals Immunoreactive Hephaestin and ferroxidase activity are present in the cytosolic fraction of rat enterocytes

BioMetals ◽  
2012 ◽  
Vol 25 (4) ◽  
pp. 687-695 ◽  
Author(s):  
Perungavur N. Ranganathan ◽  
Yan Lu ◽  
Brie K. Fuqua ◽  
James F. Collins
Keyword(s):  
Cytosolic Fraction ◽  
Ferroxidase Activity ◽  
Rat Enterocytes

scholarly journals The Ferroxidase Activity of Yeast Frataxin

2002 ◽  
Vol 277 (41) ◽  
pp. 38589-38595 ◽  
Author(s):  
Sungjo Park ◽  
Oleksandr Gakh ◽  
Steven M. Mooney ◽  
Grazia Isaya
Keyword(s):  
Ferroxidase Activity

Structure of a New Tetranuclear Iron(III) Complex with an Oxo-Bridge; Factors to Govern Formation and Stability of Oxo-Bridged Iron(III) Species in the L-Subunit of Ferritin

2006 ◽  
Vol 61 (1-2) ◽  
pp. 149-154 ◽  
Author(s):  
Yuichi Sutoh ◽  
Yuko Okawamukai ◽  
Satoshi Nishino ◽  
Yuzo Nishida
Keyword(s):  
Hydrogen Peroxide ◽  
Oxygen Atom ◽  
Electron Donor ◽  
Carboxyl Groups ◽  
Cavity Surface ◽  
Reaction Products ◽  
Ferroxidase Activity ◽  
Oxo Bridge

Abstract We have investigated the reaction products of several iron(III) compounds with hydrogen peroxide, and have found that hydrogen peroxide promotes the formation of an oxo-bridged iron(III) species in the presence of methanol (electron donor), and carboxyl groups of the ligand systems play a role to give the tetranuclear iron(III) compound containing a bent Fe- O-Fe unit (O: oxo oxygen atom). Based on the present results and the facts that L-chains of human ferritins lack ferroxidase activity, but are richer in carboxyl groups (glutamates) exposed on the cavity surface, it seems reasonable to conclude that (i) the hydrogen peroxide released in the H-subunit may contribute to the formation of a diferric oxo-hydrate in the L-subunit, (ii) the formation of a bent oxo-bridged iron(III) species is essentially important in the L-subunit, and (iii) rich carboxyl groups in L-subunits contribute to facilitate iron nucleation and mineralization through the capture and activation of the peroxide ion, and formation of a stable bent oxo-bridged iron(III) species

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