نتایج جستجو برای: ferroxidase

تعداد نتایج: 334  

Journal: :Biochemistry 2003
Guanghua Zhao Fadi Bou-Abdallah Paolo Arosio Sonia Levi Christine Janus-Chandler N Dennis Chasteen

Human ferritins sequester and store iron as a stable FeOOH((s)) mineral core within a protein shell assembled from 24 subunits of two types, H and L. Core mineralization in recombinant H- and L-subunit homopolymer and heteropolymer ferritins and several site-directed H-subunit variants was investigated to determine the iron oxidation/hydrolysis chemistry as a function of iron flux into the prot...

Journal: :The Journal of neuroscience : the official journal of the Society for Neuroscience 2011
Katrin Schulz Chris D Vulpe Leah Z Harris Samuel David

Accumulation of iron occurs in the CNS in several neurodegenerative diseases. Iron is essential for life but also has the ability to generate toxic free radicals if not properly handled. Iron homeostasis at the cellular level is therefore important to maintain proper cellular function, and its dysregulation can contribute to neurodegenerative diseases. Iron export, a key mechanism to maintain p...

Journal: :Biochemistry 2001
G Zhao F Bou-Abdallah X Yang P Arosio N D Chasteen

The ferritins are a class of iron storage and detoxification proteins that play a central role in the biological management of iron. These proteins have a catalytic site, "the ferroxidase site", located on the H-type subunit that facilitates the oxidation of Fe(II) to Fe(III) by O(2). Measurements during the past 10 years on a number of vertebrate ferritins have provided evidence that H(2)O(2) ...

Journal: :Journal of Neurology, Neurosurgery & Psychiatry 1996

Journal: :Journal of Biological Chemistry 1970

Journal: :The Journal of biological chemistry 1970
C T Huber E Frieden

The inhibitory effects of trivalent and other metal ions on f erroxidase (ceruloplasmin EC 1.12.3.1.) activity were investigated. All trivalent cations tested inhibited ferroxidase activity but the strongest inhibitors had an ionic radius of 0.81 A or less. The inhibition by Al(III) was found to be mixed competitive and uncompetitive with respect to the substrate, Fe(I1). The uncompetitive feat...

Journal: :The Biochemical journal 1995
N E Le Brun S C Andrews J R Guest P M Harrison G R Moore A J Thomson

The bacterioferritin (BFR) of Escherichia coli takes up iron in the ferrous form and stores it within its central cavity as a hydrated ferric oxide mineral. The mechanism by which oxidation of iron (II) occurs in BFR is largely unknown, but previous studies indicated that there is ferroxidase activity associated with a site capable of forming a dinuclear-iron centre within each subunit [Le Brun...

Journal: :Journal of structural biology 1999
N D Chasteen P M Harrison

Ferritins are a class of iron storage and mineralization proteins found throughout the animal, plant, and microbial kingdoms. Iron is stored within the protein shell of ferritin as a hydrous ferric oxide nanoparticle with a structure similar to that of the mineral "ferrihydrite." The eight hydrophilic channels that traverse the protein shell are thought to be the primary avenues by which iron g...

2016
Didi He Sam Hughes Sally Vanden-Hehir Atanas Georgiev Kirsten Altenbach Emma Tarrant C Logan Mackay Kevin J Waldron David J Clarke Jon Marles-Wright

Ferritins are ubiquitous proteins that oxidise and store iron within a protein shell to protect cells from oxidative damage. We have characterized the structure and function of a new member of the ferritin superfamily that is sequestered within an encapsulin capsid. We show that this encapsulated ferritin (EncFtn) has two main alpha helices, which assemble in a metal dependent manner to form a ...

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