Common NameCu(2+)
DescriptionCopper is an essential nutrient to all higher plants and animals. Physiologically, it exists as an ion in the body. In animals, it is found primarily in the bloodstream, as a cofactor in various enzymes, and in copper-based pigments. In the body, copper shifts between the cuprous (Cu1+) and cupric (Cu2+) forms, though the majority of the body's copper is in the Cu2+ form. The ability of copper to easily accept and donate electrons explains its important role in oxidation-reduction (redox) reactions and in scavenging free radicals. Copper is a critical functional component of a number of essential enzymes known as cuproenzymes. For instance, the copper-dependent enzyme, cytochrome c oxidase, plays a critical role in cellular energy production. By catalyzing the reduction of molecular oxygen (O2) to water (H2O), cytochrome c oxidase generates an electrical gradient used by the mitochondria to create the vital energy-storing molecule, ATP. Another cuproenzyme, lysyl oxidase, is required for the cross-linking of collagen and elastin, which are essential for the formation of strong and flexible connective tissue. Another cuproeznyme, Monoamine oxidase (MAO), plays a role in the metabolism of the neurotransmitters norepinephrine, epinephrine, and dopamine. MAO also functions in the degradation of the neurotransmitter serotonin, which is the basis for the use of MAO inhibitors as antidepressants. One of the most important cuproenzymes is Superoxide dismutase (SOD). SOD functions as an antioxidant by catalyzing the conversion of superoxide radicals (free radicals or ROS) to hydrogen peroxide, which can subsequently be reduced to water by other antioxidant enzymes. Two forms of SOD contain copper: 1) copper/zinc SOD is found within most cells of the body, including red blood cells, and 2) extracellular SOD is a copper-containing enzyme found at high levels in the lungs and low levels in blood plasma. In sufficient amounts, copper can be poisonous or even fatal to organisms. Copper is normally bound to cuproenzymes (such as SOD, MOA) and is thus only toxic when unsequestered and unmediated. It is believed that zinc and copper compete for absorption in the digestive tract so that a diet that is excessive in one of these minerals may result in a deficiency in the other. An imbalance of zinc and copper status might be involved in human hypertension. Furthermore, copper is found to be associated with hyperzincaemia and hypercalprotectinaemia and Wilson's disease, which are inborn errors of metabolism.
Structure
Molecular FormulaCu
Average Mass63.54600
Monoisotopic Mass62.92960
IUPAC Namecopper(2+) ion
Traditional NameCopper(2+)
CAS Registry Number7440-50-8
SMILES[Cu+2]
InChI IdentifierInChI=1S/Cu/q+2
InChI KeyJPVYNHNXODAKFH-UHFFFAOYSA-N
CHEBI IDCHEBI:29036
HMDB IDHMDB0000657
MiMeDB IDMMDBc0000133
Pathways
NameSMPDB/PathBank
Eumelanin Biosynthesis
beta-Alanine metabolism
Tyrosine metabolism
Tyrosine metabolism
Histidine metabolism
Riboflavin Metabolism
Alkaptonuria
Aromatic L-Aminoacid Decarboxylase Deficiency
Hawkinsinuria
Histidinemia
Tyrosinemia Type I
GABA-Transaminase Deficiency
Disulfiram Action Pathway
Degradation of Superoxides
Ureidopropionase Deficiency
Carnosinuria, carnosinemia
Tyrosinemia, transient, of the newborn
Tyrosine hydroxylase deficiency
Dopamine beta-hydroxylase deficiency
Monoamine oxidase-a deficiency (MAO-A)
StateSolid
Water SolubilityNot Available
logP0.16
logSNot Available
pKa (Strongest Acidic)Not Available
pKa (Strongest Basic)Not Available
Hydrogen Acceptor Count0
Hydrogen Donor Count0
Polar Surface Area0 Ų
Rotatable Bond Count0
Physiological Charge2
Formal Charge2
Refractivity0.00 m³·mol⁻¹
Polarizability1.78

We require the use of cookies for essential features like storing your previously submitted BASys2 queries. Rejecting the usage of cookies will result in certain features being disabled. By clicking ACCEPT or continuing to use the website you are agreeing to our use of cookies.

ACCEPT