Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 Fe(II) + H2O2 + 2 H2O
2 [FeO(OH)] + 4 H+
2 Fe(II) + O2 + 4 H2O
2 [FeO(OH)] + 4 H+ + H2O2
4 Fe(II) + O2 + 6 H2O
4 [FeO(OH)] + 8 H+
Fe(II) + H2O2 + H2O
[FeO(OH)] + H+
-
-
-
-
?
Fe(II) + O2 + H2O
[FeO(OH)] + H+ + H2O2
additional information
?
-
2 Fe(II) + H2O2 + 2 H2O
2 [FeO(OH)] + 4 H+
-
-
-
?
2 Fe(II) + H2O2 + 2 H2O
2 [FeO(OH)] + 4 H+
-
-
-
?
2 Fe(II) + H2O2 + 2 H2O
2 [FeO(OH)] + 4 H+
-
-
-
?
2 Fe(II) + H2O2 + 2 H2O
2 [FeO(OH)] + 4 H+
-
-
-
-
?
2 Fe(II) + H2O2 + 2 H2O
2 [FeO(OH)] + 4 H+
-
-
-
-
?
2 Fe(II) + O2 + 4 H2O
2 [FeO(OH)] + 4 H+ + H2O2
-
-
-
?
2 Fe(II) + O2 + 4 H2O
2 [FeO(OH)] + 4 H+ + H2O2
-
-
-
?
2 Fe(II) + O2 + 4 H2O
2 [FeO(OH)] + 4 H+ + H2O2
-
-
-
?
2 Fe(II) + O2 + 4 H2O
2 [FeO(OH)] + 4 H+ + H2O2
-
-
-
-
?
2 Fe(II) + O2 + 4 H2O
2 [FeO(OH)] + 4 H+ + H2O2
-
-
-
-
?
4 Fe(II) + O2 + 6 H2O
4 [FeO(OH)] + 8 H+
-
-
-
?
4 Fe(II) + O2 + 6 H2O
4 [FeO(OH)] + 8 H+
overall reaction
-
-
?
4 Fe(II) + O2 + 6 H2O
4 [FeO(OH)] + 8 H+
-
-
-
?
4 Fe(II) + O2 + 6 H2O
4 [FeO(OH)] + 8 H+
overall reaction
-
-
?
Fe(II) + O2 + H2O
[FeO(OH)] + H+ + H2O2
-
-
-
?
Fe(II) + O2 + H2O
[FeO(OH)] + H+ + H2O2
-
-
-
?
Fe(II) + O2 + H2O
[FeO(OH)] + H+ + H2O2
-
-
-
?
Fe(II) + O2 + H2O
[FeO(OH)] + H+ + H2O2
-
-
-
?
Fe(II) + O2 + H2O
[FeO(OH)] + H+ + H2O2
-
-
-
-
?
Fe(II) + O2 + H2O
[FeO(OH)] + H+ + H2O2
-
-
-
?
Fe(II) + O2 + H2O
[FeO(OH)] + H+ + H2O2
-
-
-
-
?
Fe(II) + O2 + H2O
[FeO(OH)] + H+ + H2O2
-
overall reaction
-
-
?
Fe(II) + O2 + H2O
[FeO(OH)] + H+ + H2O2
-
-
-
?
Fe(II) + O2 + H2O
[FeO(OH)] + H+ + H2O2
-
-
-
?
Fe(II) + O2 + H2O
[FeO(OH)] + H+ + H2O2
-
-
-
-
?
additional information
?
-
the formation of the iron hydroxide core is monitored spectrophotometrically at 305 nm. The enzyme is able to bind DNA, DNA-binding analysis fro wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
the formation of the iron hydroxide core is monitored spectrophotometrically at 305 nm. The enzyme is able to bind DNA, DNA-binding analysis fro wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
although H2O2 is a product of dioxygen reduction in FtnA and oxidation occurs with a stoichiometry of Fe2+/O2 about 3:1 most of the H2O2 produced is consumed in subsequent reactions with a 2:1 Fe2+/H2O2 stoichiometry, thus suppressing hydroxyl-radical formation
-
-
?
additional information
?
-
in addition to the conserved A- and B-sites of the diiron ferroxidase center, EcFtnA has a third iron-binding site (the C-site) that is near the diiron site. The enzyme requires fully functional A- and B-sites for high ferroxidase activity. There are multiple iron-oxidation pathways in EcFtnA with O2 and H2O2 as oxidants. While H2O2 is a product of dioxygen reduction in EcFtnA and oxidation occurs with a stoichiometry of Fe(II)/O2 about 3:1, most of the H2O2 produced is consumed in subsequent reactions with a 2:1 Fe(II)/H2O2 stoichiometry, thus suppressing hydroxyl radical formation. One of the unique properties of EcFtnA is its unusual Fe(II)/O2 oxidation stoichiometry of approx. 3
-
-
?
additional information
?
-
-
in addition to the conserved A- and B-sites of the diiron ferroxidase center, EcFtnA has a third iron-binding site (the C-site) that is near the diiron site. The enzyme requires fully functional A- and B-sites for high ferroxidase activity. There are multiple iron-oxidation pathways in EcFtnA with O2 and H2O2 as oxidants. While H2O2 is a product of dioxygen reduction in EcFtnA and oxidation occurs with a stoichiometry of Fe(II)/O2 about 3:1, most of the H2O2 produced is consumed in subsequent reactions with a 2:1 Fe(II)/H2O2 stoichiometry, thus suppressing hydroxyl radical formation. One of the unique properties of EcFtnA is its unusual Fe(II)/O2 oxidation stoichiometry of approx. 3
-
-
?
additional information
?
-
-
in bacterioferritin, iron mineralization kinetics are dependent on an intra-subunit catalytic diiron cofactor site (the ferroxidase centre), three closely located aromatic residues and an inner surface iron site. One of the aromatic residues, Tyr25, is the site of formation of a transient radical. The other two residues are Tyr58 and Trp133, these residues are important for the rates of formation and decay of the Tyr25 radical and decay of a secondary radical observed during Tyr25 radical decay. Mechanism in which these aromatic residues function in electron transfer from the inner surface site to the ferroxidase centre, overview
-
-
?
additional information
?
-
-
addition of 2 Fe2+ ions per subunit or 4 Fe2+ ions per subunit in frog wild-type or H54A mutant M ferritin. Recombinant ferritin protein cages are mineralized with ferrous sulfate, 20 Fe2+ ions per subunit. Fe2+ exit from caged ferritin minerals is initiated by reducing the ferritin mineral with added NADH and FMN and trapping the reduced and dissolved Fe2+ as the [Fe(2,2'-bipyridyl)3]2+ complex outside the protein cage. Fe2+ release from the protein cage is measured as the absorbance of [Fe(2,2'-bipyridyl)3]2+ at the maximum of A522 nm
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Alzheimer Disease
Association of A beta 40-positive senile plaques with microglial cells in the brains of patients with Alzheimer's disease and in non-demented aged individuals.
Anemia
Cost-effective paper-based electrochemical immunosensor using a label-free assay for sensitive detection of ferritin.
Anemia, Iron-Deficiency
Cost-effective paper-based electrochemical immunosensor using a label-free assay for sensitive detection of ferritin.
Arthritis
Placental immunomodulator ferritin, a novel immunoregulator, suppresses experimental arthritis.
Atherosclerosis
Is increased tissue ferritin a risk factor for atherosclerosis and ischaemic heart disease?
Bacteremia
Differential gene expression in Streptococcus pneumoniae in response to various iron sources.
Breast Neoplasms
Immunological reactivity of serum ferritin in patients with malignancy.
Carcinoma
Ferritin: A potential serum marker for lymph node metastasis in head and neck squamous cell carcinoma.
Carcinoma
Ferritin: a tumor marker expressed by renal cell carcinoma.
Carcinoma
Serum ferritin: a tumor marker for renal cell carcinoma.
Carcinoma, Renal Cell
Ferritin: a tumor marker expressed by renal cell carcinoma.
Carcinoma, Renal Cell
Serum ferritin: a tumor marker for renal cell carcinoma.
Carcinoma, Squamous Cell
Ferritin: A potential serum marker for lymph node metastasis in head and neck squamous cell carcinoma.
Cardiovascular Diseases
Angiotensin II alters the expression of duodenal iron transporters, hepatic hepcidin, and body iron distribution in mice.
Cataract
Bilateral cataract and high serum ferritin: a new dominant genetic disorder?
Coronary Disease
Serum Ferritin Levels in Blacks Without Known Cardiovascular Disease (from the Jackson Heart Study).
Dengue
Serum Ferritin: A Backstage Weapon in Diagnosis of Dengue Fever.
Diabetes Mellitus
Ferritin modifies the relationship between inflammation and arterial stiffness in hypertensive patients with different glucose tolerance.
Diabetes Mellitus, Type 2
Cardiovascular risk factors in non-insulin-dependent diabetics compared to non-diabetic controls: a population-based survey among Asians in Singapore.
Diabetes Mellitus, Type 2
Circulating ferritin concentrations and risk of type 2 diabetes in Japanese individuals.
Diabetes Mellitus, Type 2
Elevated plasma ferritin is associated with increased incidence of type 2 diabetes in middle-aged and elderly chinese adults.
Diabetes Mellitus, Type 2
Ferritin modifies the relationship between inflammation and arterial stiffness in hypertensive patients with different glucose tolerance.
Diabetes Mellitus, Type 2
Serum Transferrin Predicts New-Onset Type 2 Diabetes in Koreans: A 4-Year Retrospective Longitudinal Study.
Enteritis
Campylobacter jejuni DNA-binding protein from starved cells in Guillain-Barré syndrome patients.
Hodgkin Disease
Ferritin, a Hodgkin's disease associated antigen.
Hodgkin Disease
Immunological reactivity of serum ferritin in patients with malignancy.
Hyperferritinemia
The iron-heart disease connection: is it dead or just hiding?
Hyperferritinemia
Unexplained isolated hyperferritinemia without iron overload.
Hypertension
Angiotensin II alters the expression of duodenal iron transporters, hepatic hepcidin, and body iron distribution in mice.
Hypertension
Ferritin modifies the relationship between inflammation and arterial stiffness in hypertensive patients with different glucose tolerance.
Infections
Helicobacter pylori infection and serum ferritin: A population-based study among 1806 adults in Germany.
Insulin Resistance
Insulin resistance, atherogenicity, and iron metabolism in multiple sclerosis with and without depression: Associations with inflammatory and oxidative stress biomarkers and uric acid.
Insulin Resistance
Serum ferritin is associated with markers of insulin resistance in Japanese men but not in women.
Iron Deficiencies
A photonic crystal biosensor assay for ferritin utilizing iron-oxide nanoparticles.
Iron Deficiencies
Ferritin, a faithful reflection of iron deficiency in IUD wearers with mild vaginal spotting.
Iron Deficiencies
Red cell ferritin, a marker of iron deficiency in hemodialysis patients.
Iron Deficiencies
Urinary ferritin; a potential noninvasive way to screen NICU patients for iron deficiency.
Iron Overload
Iron overload adversely affects outcome of allogeneic hematopoietic cell transplantation.
Iron Overload
Iron Overload Coordinately Promotes Ferritin Expression and Fat Accumulation in Caenorhabditis elegans.
Iron Overload
Iron overload in patients undergoing hematopoietic stem cell transplantation.
Leukemia
Immunological reactivity of serum ferritin in patients with malignancy.
Leukemia, Myeloid, Acute
Immunological reactivity of serum ferritin in patients with malignancy.
Lung Neoplasms
Immunological reactivity of serum ferritin in patients with malignancy.
Lymphatic Metastasis
Ferritin: A potential serum marker for lymph node metastasis in head and neck squamous cell carcinoma.
Lymphohistiocytosis, Hemophagocytic
Low glycosylated ferritin, a good marker for the diagnosis of hemophagocytic syndrome.
Lymphoma
Ferritin, a sensitizing substance in the leucocyte migration inhibition test in patients with malignant lymphoma.
Metabolic Syndrome
Serum ferritin levels are associated with metabolic syndrome in postmenopausal women but not in premenopausal women.
Metrorrhagia
Ferritin, a faithful reflection of iron deficiency in IUD wearers with mild vaginal spotting.
Myelodysplastic Syndromes
Serum ferritin levels at diagnosis predict prognosis in patients with low blast count myelodysplastic syndromes.
Myocardial Infarction
The iron-heart disease connection: is it dead or just hiding?
Neoplasm Metastasis
Ferritin: A potential serum marker for lymph node metastasis in head and neck squamous cell carcinoma.
Neoplasms
Development of an immunosensor for human ferritin, a nonspecific tumor marker, based on surface plasmon resonance.
Neoplasms
Ferritin: a tumor marker expressed by renal cell carcinoma.
Neoplasms
Mitochondrial ferritin, a new target for inhibiting neuronal tumor cell proliferation.
Neoplasms
Monoclonal and polyclonal antibodies against human ferritin, a nonspecific tumor marker.
Neoplasms
Serum ferritin: a tumor marker for renal cell carcinoma.
Neoplasms
[Peptide aptamers and nano-carriers for cancer therapy]
Neurodegenerative Diseases
Apoferritin Protein Amyloid Fibrils with Tunable Chirality and Polymorphism.
Neurodegenerative Diseases
Evaluation of ferritin-overexpressing brain in newly developed transgenic mice.
Obesity
Iron Overload Coordinately Promotes Ferritin Expression and Fat Accumulation in Caenorhabditis elegans.
Pneumonia
Differential gene expression in Streptococcus pneumoniae in response to various iron sources.
Restless Legs Syndrome
Efficacy of oral iron in patients with restless legs syndrome and a low-normal ferritin: A randomized, double-blind, placebo-controlled study.
Squamous Cell Carcinoma of Head and Neck
Ferritin: A potential serum marker for lymph node metastasis in head and neck squamous cell carcinoma.
Starvation
Ferritin-like family proteins in the anaerobe Bacteroides fragilis: when an oxygen storm is coming, take your iron to the shelter.
Starvation
The DNA-Binding Protein from Starved Cells (Dps) Utilizes Dual Functions To Defend Cells against Multiple Stresses.
Tuberculosis
Mycobacterium tuberculosis ferritin: a suitable workhorse protein for cryo-EM development.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
Dps (DNA-binding protein from starved cells) belongs to a subfamily of ferritins. The presence of a ferroxidase centre, composed of highly conserved residues, is a signature of this protein family
evolution
-
the ferritin (Ftn) and bacterioferritin (Bfr) proteins of the ferritin-like superfamily constitute a prime example of a remarkable combination of evolutionary conserved iron uptake and release processes that are integrated with a variety in iron translocation mechanisms. Ftns and Bfrs have a highly conserved architecture
evolution
-
the ferritin (Ftn) and bacterioferritin (Bfr) proteins of the ferritin-like superfamily constitute a prime example of a remarkable combination of evolutionary conserved iron uptake and release processes that are integrated with a variety in iron translocation mechanisms. Ftns and Bfrs have a highly conserved architecture
evolution
-
Dps (DNA-binding protein from starved cells) belongs to a subfamily of ferritins. The presence of a ferroxidase centre, composed of highly conserved residues, is a signature of this protein family
-
physiological function
-
the major iron-storage protein ferritin A in Escherichia coli acts as an iron buffer for re-assembly of iron-sulfur clusters in response to hydrogen peroxide stress. The iron stored in ferritin A can be retrieved by an iron chaperon IscA for the re-assembly of the iron-sulfur cluster in a proposed scaffold IscU in the presence of the thioredoxin reductase system which emulates normal intracellular redox potential
physiological function
Dps proteins are widely distributed in being required for survival during stressful conditions such as nutrient starvation, thermal stress and oxidative conditions, and inside biofilm. Campylobacter jejuni needs to be able to counteract various types of environmental stress during colonization, for example extreme pH and low availability of trace metals such as iron. Dps proteins can store iron atoms inside the dodecamer. Campylobacter jejuni Dps is able to bind DNA, and the DNA-binding activity is stimulated by Fe2+ (at room temperature in Bis-Tris, pH 6.0), overview
physiological function
-
ferritin and ferritin-like molecules (Bfr and bacterial Ftn) are supramolecular assemblies built from 24 subunits into a nearly spherical architecture with a hollow core where up to 4000 iron ions can be stored as a ferric mineral that is protected from indiscriminant cellular reducing agents. The enzymes possess an integrated ferroxidase activity, EC 1.16.3.1. . Network-weaving algorithm that passes threads of an allosteric network through highly correlated residues using hierarchical clustering, the residue-residue correlations are calculated, modeling, overview. The ferritin structures evolved in a way to limit the influence of functionally unrelated events in the cytoplasm on the allosteric network to maintain stability of the translocation mechanisms. Diversity in mechanisms of iron traffic, overview. It is thought that iron translocation across the ferritin shell requires cooperative motions of residues aligning the path. In the process of iron capture and storage, iron traverses from the ferritin exterior surface to the interior cavity via a ferroxidase center, where soluble Fe2+ is oxidized to Fe3+. A ferroxidase center is located in the middle of each subunit in the heavy (H)-type and M-type subunits of eukaryotic Ftns. Release of iron from the ferritin cavity requires reduction of ferric iron in the interior ferritin cavity and egress of ferrous ions via pores in the protein shell. The networks in BfrB and FtnA connect the ferroxidase center with the 4fold pores and B-pores, leaving the 3fold pores unengaged
physiological function
-
ferritin and ferritin-like molecules (Bfr and bacterial Ftn) are supramolecular assemblies built from 24 subunits into a nearly spherical architecture with a hollow core where up to 4000 iron ions can be stored as a ferric mineral that is protected from indiscriminant cellular reducing agents. The enzymes possess an integrated ferroxidase activity, EC 1.16.3.1. Network-weaving algorithm that passes threads of an allosteric network through highly correlated residues using hierarchical clustering, the residue-residue correlations are calculated, modeling, overview. Each type of ferritin-like molecule has an extended network of highly correlated residues, connecting distant pores and the ferroxidase center. The ferritin structures evolved in a way to limit the influence of functionally unrelated events in the cytoplasm on the allosteric network to maintain stability of the translocation mechanisms. Diversity in mechanisms of iron traffic, overview. It is thought that iron translocation across the ferritin shell requires cooperative motions of residues aligning the path. In the process of iron capture and storage, iron traverses from the ferritin exterior surface to the interior cavity via a ferroxidase center, where soluble Fe2+ is oxidized to Fe3+. A ferroxidase center is located in the middle of each subunit in Bfrs. Release of iron from the ferritin cavity requires reduction of ferric iron in the interior ferritin cavity and egress of ferrous ions via pores in the protein shell. The networks in BfrB and FtnA connect the ferroxidase center with the 4fold pores and B-pores, leaving the 3fold pores unengaged
physiological function
-
ferritin and ferritin-like molecules (Bfr and bacterial Ftn) are supramolecular assemblies built from 24 subunits into a nearly spherical architecture with a hollow core where up to 4000 iron ions can be stored as a ferric mineral that is protected from indiscriminant cellular reducing agents. The enzymes possess an integrated ferroxidase activity, EC 1.16.3.1. Network-weaving algorithm that passes threads of an allosteric network through highly correlated residues using hierarchical clustering, the residue-residue correlations are calculated, modeling, overview. Each type of ferritin-like molecule has an extended network of highly correlated residues, connecting distant pores and the ferroxidase center. The ferritin structures evolved in a way to limit the influence of functionally unrelated events in the cytoplasm on the allosteric network to maintain stability of the translocation mechanisms. Diversity in mechanisms of iron traffic, overview. It is thought that iron translocation across the ferritin shell requires cooperative motions of residues aligning the path. In the process of iron capture and storage, iron traverses from the ferritin exterior surface to the interior cavity via a ferroxidase center, where soluble Fe2+ is oxidized to Fe3+. A ferroxidase center is located in the middle of each subunit in bacterial Ftn. Release of iron from the ferritin cavity requires reduction of ferric iron in the interior ferritin cavity and egress of ferrous ions via pores in the protein shell. The networks in BfrB and FtnA connect the ferroxidase center with the 4fold pores and B-pores, leaving the 3fold pores unengaged
physiological function
ferritins use Fe2+ and either dioxygen or hydrogen peroxide as oxidants to form a hydrous ferric oxide mineral core. The enzyme EcFtnA displays H2O2 detoxification properties whereby two Fe2+ are oxidized per H2O2 reduced. The enzyme requires fully functional A- and B-sites for high ferroxidase activity. The mechanism of iron oxidation and deposition in EcFtnA is complex with multiple reactions involving the A-, B-, and C-sites of the ferroxidase center, the mineral surface and both O2 and H2O2 as oxidants
physiological function
-
Dps proteins are widely distributed in being required for survival during stressful conditions such as nutrient starvation, thermal stress and oxidative conditions, and inside biofilm. Campylobacter jejuni needs to be able to counteract various types of environmental stress during colonization, for example extreme pH and low availability of trace metals such as iron. Dps proteins can store iron atoms inside the dodecamer. Campylobacter jejuni Dps is able to bind DNA, and the DNA-binding activity is stimulated by Fe2+ (at room temperature in Bis-Tris, pH 6.0), overview
-
additional information
-
iron mineralization kinetics
additional information
-
role for His54 as a metal ion trap that maintains the correct levels of access of iron to the active site. His54 binding to iron(II) and other divalent cations, with its imidazole ring proposed as gate that influences iron movement to/from the active site.
additional information
two conserved histidine residues, H25 and H37, located at the ferroxidase centre of the Campylobacter jejuni Dps (DNA-binding protein from starved cells) protein, are not strictly required for metal binding and oxidation. The archetypical function of Dps seems to be DNA protection against hydroxyl radicals that are produced when Fe2+ and H2O2 combine
additional information
-
two conserved histidine residues, H25 and H37, located at the ferroxidase centre of the Campylobacter jejuni Dps (DNA-binding protein from starved cells) protein, are not strictly required for metal binding and oxidation. The archetypical function of Dps seems to be DNA protection against hydroxyl radicals that are produced when Fe2+ and H2O2 combine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
H25G
site-directed mutagenesis, the mutant is able to accumulate iron in its inner cavity similar to the wild-type enzyme
H25G/H37G
site-directed mutagenesis, the mutant shows reduced activity to accumulate iron in its inner cavity compared to the wild-type enzyme
H37G
site-directed mutagenesis, the mutant is able to accumulate iron in its inner cavity similar to the wild-type enzyme
H25G
-
site-directed mutagenesis, the mutant is able to accumulate iron in its inner cavity similar to the wild-type enzyme
-
H25G/H37G
-
site-directed mutagenesis, the mutant shows reduced activity to accumulate iron in its inner cavity compared to the wild-type enzyme
-
H37G
-
site-directed mutagenesis, the mutant is able to accumulate iron in its inner cavity similar to the wild-type enzyme
-
W133F
-
the Tyr25 radical spectrum simulated for the radical in the wild-type protein is overlaid with the difference spectrum proposed to originate from the same species in the mutant variant, overview
Y24F
site-directed mutagenesis, variant Y24F is a kinetically competent protein capable of forming a diFe(III) peroxo complex upon addition of the first 48 Fe(II) to the protein with rate parameters similar to wild-type EcFtnA
H54A
-
site-directed mutagenesis, the mutant variant exhibits a 20% increase in the initial reaction rate of formation of ferric products with 2 or 4 Fe2+/subunit and higher than 200% with 20 Fe2+/subunit. The increased efficiency of the ferritin reaction induced by this mutation is proposed taking advantage of the comparative sequence analysis of other ferritins
E129C
-
the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme
E129Q
-
the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme
E129R
-
the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme
E130H
-
the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme
E17H
-
the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme
E50H
-
the mutant shows severely reduced iron oxidation rate compared to the wild type enzyme
E126A
-
the mutation causes a decrease in the Fe2+/O2 stoichiometry from about 3 to about 2 for the first 48 Fe2+ added to the protein
E126A
site-directed mutagenesis, elimination of C-site ligands as in variants E126A, E49A and E130A causes a decrease in the Fe(II)/O2 stoichiometry from approx. 3 to approx. 2 for the first 48 Fe(II) added to the protein. The C-site variants (particularly E49A and E126A) fully regenerate their initial ferroxidase activity within a few hours compared to a day or so required for wild-type EcFtnA
E130A
-
the mutation causes a decrease in the Fe2+/O2 stoichiometry from about 3 to about 2 for the first 48 Fe2+ added to the protein
E130A
site-directed mutagenesis, elimination of C-site ligands as in variants E126A, E49A and E130A causes a decrease in the Fe(II)/O2 stoichiometry from approx. 3 to approx. 2 for the first 48 Fe(II) added to the protein
E17A
-
the mutation increases the Fe2+/O2 stoichiometry from about 3 to about 4 compared to the wild type enzyme
E17A
site-directed mutagenesis, elimination of either A- or B-site ligands of EcFtnA, as in variants H53A, E17A and E94A, increases the Fe(II)/O2 stoichiometry from approx. 3 to approx. 4
E49A
-
the mutation causes a decrease in the Fe2+/O2 stoichiometry from about 3 to about 2 for the first 48 Fe2+ added to the protein
E49A
site-directed mutagenesis, elimination of C-site ligands as in variants E126A, E49A and E130A causes a decrease in the Fe(II)/O2 stoichiometry from approx. 3 to approx. 2 for the first 48 Fe(II) added to the protein. The C-site variants (particularly E49A and E126A) fully regenerate their initial ferroxidase activity within a few hours compared to a day or so required for wild-type EcFtnA
E94A
-
the mutation increases the Fe2+/O2 stoichiometry from about 3 to about 4 compared to the wild type enzyme
E94A
site-directed mutagenesis, elimination of either A- or B-site ligands of EcFtnA, as in variants H53A, E17A and E94A, increases the Fe(II)/O2 stoichiometry from approx. 3 to approx. 4
H53A
-
the mutation increases the Fe2+/O2 stoichiometry from about 3 to about 4 compared to the wild type enzyme
H53A
site-directed mutagenesis, elimination of either A- or B-site ligands of EcFtnA, as in variants H53A, E17A and E94A, increases the Fe(II)/O2 stoichiometry from approx. 3 to approx. 4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Bauminger, E.R.; Treffry, A.; Quail, M.A.; Zhao, Z.; Nowik, I.; Harrison, P.M.
Stages in iron storage in the ferritin of Escherichia coli (EcFtnA): analysis of Moessbauer spectra reveals a new intermediate
Biochemistry
38
7791-7802
1999
Escherichia coli
brenda
Bou-Abdallah, F.; Yang, H.; Awomolo, A.; Cooper, B.; Woodhall, M.; Andrews, S.; Chasteen, N.
Functionality of the three-site ferroxidase center of Escherichia coli bacterial ferritin (EcFtnA)
Biochemistry
53
483-495
2014
Escherichia coli
brenda
Reindel, S.; Anemueller, S.; Sawaryn, A.; Matzanke, B.F.
The DpsA-homologue of the archaeon Halobacterium salinarum is a ferritin
Biochim. Biophys. Acta
1598
140-146
2002
Halobacterium salinarum (Q9HMP7), Halobacterium salinarum, Halobacterium salinarum NRC 1 (Q9HMP7)
brenda
Bitoun, J.P.; Wu, G.; Ding, H.
Escherichia coli FtnA acts as an iron buffer for re-assembly of iron-sulfur clusters in response to hydrogen peroxide stress
Biometals
21
693-703
2008
Escherichia coli
brenda
Rocha, E.R.; Smith, C.J.
Ferritin-like family proteins in the anaerobe Bacteroides fragilis: when an oxygen storm is coming, take your iron to the shelter
Biometals
26
577-591
2013
Bacteroides fragilis (E1WS50), Bacteroides fragilis (P0CJ83), Bacteroides fragilis (Q5LBE2), Bacteroides fragilis, Bacteroides fragilis 638R (E1WS50), Bacteroides fragilis NCTC 9343 (Q5LBE2), Bacteroides fragilis YCH46 (P0CJ83)
brenda
Hudson, A.; Andrews, S.; Hawkins, C.; Williams, J.; Izuhara, M.; Meldrum, F.; Mann, S.; Harrison, P.; Guest, J.
Overproduction, purification and characterization of the Escherichia coli ferritin
Eur. J. Biochem.
218
985-995
1993
Escherichia coli (P0A998)
brenda
Stillman, T.J.; Hempstead, P.D.; Artymiuk, P.J.; Andrews, S.C.; Hudson, A.J.; Treffry, A.; Guest, J.R.; Harrison, P.M.
The high-resolution X-ray crystallographic structure of the ferritin (EcFtnA) of Escherichia coli; comparison with human H ferritin (HuHF) and the structures of the Fe(3+) and Zn(2+) derivatives
J. Mol. Biol.
307
587-603
2001
Escherichia coli (P0A998), Escherichia coli
brenda
Honarmand Ebrahimi, K.; Bill, E.; Hagedoorn, P.L.; Hagen, W.R.
The catalytic center of ferritin regulates iron storage via Fe(II)-Fe(III) displacement
Nat. Chem. Biol.
8
941-948
2012
Pyrococcus furiosus
brenda
Sevcenco, A.M.; Paravidino, M.; Vrouwenvelder, J.S.; Wolterbeek, H.T.; van Loosdrecht, M.C.; Hagen, W.R.
Phosphate and arsenate removal efficiency by thermostable ferritin enzyme from Pyrococcus furiosus using radioisotopes
Water Res.
76
181-186
2015
Pyrococcus furiosus
brenda
Bou-Abdallah, F.; Yang, H.; Awomolo, A.; Cooper, B.; Woodhall, M.R.; Andrews, S.C.; Chasteen, N.D.
Functionality of the three-site ferroxidase center of Escherichia coli bacterial ferritin (EcFtnA)
Biochemistry
53
483-495
2014
Escherichia coli (P0A998), Escherichia coli
brenda
Bernacchioni, C.; Ciambellotti, S.; Theil, E.C.; Turano, P.
Is His54 a gating residue for the ferritin ferroxidase site?
Biochim. Biophys. Acta
1854
1118-1122
2015
Lithobates catesbeianus
brenda
Ruvinsky, A.; Vakser, I.; Rivera, M.
Local packing modulates diversity of iron pathways and cooperative behavior in eukaryotic and prokaryotic ferritins
J. Chem. Phys.
140
115104
2014
Pseudomonas aeruginosa, Lithobates catesbeianus
brenda
Bradley, J.M.; Svistunenko, D.A.; Moore, G.R.; Le Brun, N.E.
Tyr25, Tyr58 and Trp133 of Escherichia coli bacterioferritin transfer electrons between iron in the central cavity and the ferroxidase centre
Metallomics
9
1421-1428
2017
Escherichia coli
brenda
Sanchuki, H.B.; Valdameri, G.; Moure, V.R.; Rodriguez, J.A.; Pedrosa, F.O.; Souza, E.M.; Korolik, V.; Ribeiro, R.R.; Huergo, L.F.
Conserved histidine residues at the ferroxidase centre of the Campylobacter jejuni Dps protein are not strictly required for metal binding and oxidation
Microbiology
162
156-163
2016
Campylobacter jejuni subsp. jejuni (Q0P891), Campylobacter jejuni subsp. jejuni ATCC 700819 (Q0P891)
brenda