Page last updated: 2024-10-24

ferric iron binding

Definition

Target type: molecularfunction

Binding to a ferric iron ion, Fe(III). [GOC:ai]

Ferric iron binding is a molecular function that describes the ability of a protein or molecule to bind to ferric iron (Fe3+), the oxidized form of iron. This binding process is crucial for a variety of biological functions, including:

- **Electron transfer:** Ferric iron is an important component of electron transport chains, which are involved in energy production in cells.
- **Oxygen transport:** Hemoglobin, the protein responsible for oxygen transport in blood, binds to ferric iron.
- **Enzyme activity:** Many enzymes require ferric iron as a cofactor to function properly. For example, cytochrome P450 enzymes, which play a role in detoxification and metabolism, use ferric iron to catalyze reactions.
- **Iron storage and transport:** Proteins like ferritin and transferrin bind to ferric iron to store and transport it throughout the body.
- **Redox regulation:** Ferric iron can participate in redox reactions, where it can be oxidized or reduced. This property is important for various cellular processes.

The binding of ferric iron to proteins or molecules is typically facilitated by specific amino acid residues that coordinate with the iron ion. These residues often include histidine, aspartate, glutamate, and tyrosine, which can form strong electrostatic interactions with the ferric ion.

The strength of the interaction between the iron ion and the protein or molecule can vary depending on the specific binding site and the surrounding environment. This strength is important for determining the function and stability of the iron-binding complex.'
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Proteins (2)

ProteinDefinitionTaxonomy
Ribonucleoside-diphosphate reductase subunit M2A ribonucleoside-diphosphate reductase subunit M2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P31350]Homo sapiens (human)
Tyrosine 3-monooxygenaseA tyrosine 3-monooxygenase that is encoded in the genome of human. [PRO:DNx, UniProtKB:P07101]Homo sapiens (human)

Compounds (7)

CompoundDefinitionClassesRoles
uridine diphosphateUridine Diphosphate: A uracil nucleotide containing a pyrophosphate group esterified to C5 of the sugar moiety.pyrimidine ribonucleoside 5'-diphosphate;
uridine 5'-phosphate
Escherichia coli metabolite;
mouse metabolite
cytidine diphosphateCytidine Diphosphate: Cytidine 5'-(trihydrogen diphosphate). A cytosine nucleotide containing two phosphate groups esterified to the sugar moiety. Synonyms: CRPP; cytidine pyrophosphate.cytidine 5'-phosphate;
pyrimidine ribonucleoside 5'-diphosphate
Escherichia coli metabolite;
mouse metabolite
n-n-propylnorapomorphineaporphine alkaloid
monoiodotyrosine3-iodo-L-tyrosine : The monoiodotyrosine that is L-tyrosine carrying an iodo-substituent at position C-3 of the benzyl group.

iodotyrosine : A tyrosine derivative which has at least one iodo-substituent on the benzyl moiety.

monoiodotyrosine : An iodotyrosine carrying a single iodo substituent.

Monoiodotyrosine: A product from the iodination of tyrosine. In the biosynthesis of thyroid hormones (THYROXINE and TRIIODOTHYRONINE), tyrosine is first iodized to monoiodotyrosine.
amino acid zwitterion;
L-tyrosine derivative;
monoiodotyrosine;
non-proteinogenic L-alpha-amino acid
EC 1.14.16.2 (tyrosine 3-monooxygenase) inhibitor;
human metabolite;
mouse metabolite
1-aminoadenosine1-aminoadenosine: structure
3-aminopyridine-2-carboxaldehyde thiosemicarbazone3-aminopyridine-2-carboxaldehyde thiosemicarbazone: a neuroprotective agent; structure given in first source
11-hydroxy-n-(n-propyl)noraporphine hydrochloride, (r)-isomer