Information about Metalloprotein
In biochemistry, a metalloprotein is a generic term for a protein that contains a metal cofactor. The metal may be an isolated ion or may be coordinated with a nonprotein organic compound, such as the porphyrin found in hemoproteins. In some cases, the metal is co-coordinated with a side chain of the protein and an inorganic nonmetallic ion. This kind of protein-metal-nonmetal structure is seen in iron-sulfur clusters.
An important class of metalloproteins are metalloenzymes, these are enzymes that contain one or more metal atoms as functional parts of their structures. These metals are often involved in enzyme catalysis, such as in carbonic anhydrase and cytochrome c oxidase. Metal ions usually form part of the active site as they can be multicoordinated and thus held in a protein while having a high affinity for the substrate through a lone pair.
An important class of metalloproteins are metalloenzymes, these are enzymes that contain one or more metal atoms as functional parts of their structures. These metals are often involved in enzyme catalysis, such as in carbonic anhydrase and cytochrome c oxidase. Metal ions usually form part of the active site as they can be multicoordinated and thus held in a protein while having a high affinity for the substrate through a lone pair.
List of metalloenzymes
| Ion | Examples of enzymes containing this ion |
|---|---|
| Cupric | Cytochrome oxidase |
| Ferrous or Ferric | Catalase Cytochrome(via Heme) Nitrogenase Hydrogenase |
| Nickel | Urease |
| Selenium | Glutathione peroxidase |
| Zinc | Alcohol dehydrogenase Carbonic anhydrase DNA polymerase |
See also
References
Biochemistry is the study of the chemical processes in living organisms.[1] The word "biochemistry" comes from the Greek word βιοχημεία biochēmeia, which means "the chemistry of life.
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Proteins are large organic compounds made of amino acids arranged in a linear chain and joined together by peptide bonds between the carboxyl and amino groups of adjacent amino acid residues.
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The Macro Expansion Template Attribute Language complements TAL, providing macros which allow the reuse of code across template files. Both were created for Zope but are used in other Python projects as well.
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EC1 Oxidoreductases/list - EC2 Transferases/list - EC3 Hydrolases/list - EC4 Lyases/list - EC5 Isomerases/list - EC6 Ligases/list
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ion is an atom or molecule which has lost or gained one or more electrons, making it positively or negatively charged. A negatively charged ion, which has more electrons in its electron shells than it has protons in its nuclei, is known as an anion
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Organometallic chemistry is the study of chemical compounds containing bonds between carbon and a metal.[1] Since many compounds without such bonds are chemically similar, an alternative may be compounds containing metal-element bonds of a largely covalent character.
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porphyrin is a heterocyclic macrocycle derived from four pyrrole-like subunits interconnected via their α carbon atoms via methine bridges (=CH-). The macrocycle, therefore, is a highly conjugated system, and is consequently deeply coloured—the name porphyrin
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A hemoprotein (also haemoprotein), or heme protein, is a metalloprotein containing a heme prosthetic group, either covalently or noncovalently bound to the protein itself.
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side chain in organic chemistry and biochemistry is a part of a molecule that is attached to a core structure. An R group is a generic label for a side chain which can be anything; however, it is typically stable and covalently linked to the adjoining atom.
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An iron-sulfur cluster is a structural motif found in a variety of metalloproteins, such as the ferredoxins, as well as NADH dehydrogenase and Coenzyme Q - cytochrome c reductase, and nitrogenase.
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Enzymes are proteins that catalyze (i.e. accelerate) chemical reactions.[1] In enzymatic reactions, the molecules at the beginning of the process are called substrates, and the enzyme converts them into different molecules, the products.
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Enzyme catalysis is the catalysis of chemical reactions by specialized proteins, enzymes. Catalysis of biochemical reactions in the cell is vital due to the very low reaction rates of the uncatalysed reactions.
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Carbonic anhydrase (carbonate dehydratase) is a family of metalloenzymes (enzymes that contain one or more metal atoms as a functional component of the enzyme) that catalyze the rapid conversion of carbon dioxide to bicarbonate and protons, a reaction that occurs rather
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cytochrome c oxidase or Complex IV (PDB 2OCC , EC 1.9.3.1 ) is a large transmembrane protein complex found in bacteria and the mitochondrion.
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Function
It is the last protein in the electron transport chain...... Click the link for more information.
The active site of an enzyme contains the catalytic and binding sites. The structure and chemical properties of the active site allow the recognition and binding of the substrate.
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A lone pair is a (valence) electron pair without bonding or sharing with other atoms. They are found in the outermost electron shell of an atom, so lone pairs are a subset of a molecule's valence electrons.
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2, 1
(mildly basic oxide)
Electronegativity 1.90 (Pauling scale)
Ionization energies
(more) 1st: 745.5 kJmol−1
2nd: 1957.9 kJmol−1
3rd: 3666 kJmol−1
Atomic radius 135 pm
Atomic radius (calc.
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(mildly basic oxide)
Electronegativity 1.90 (Pauling scale)
Ionization energies
(more) 1st: 745.5 kJmol−1
2nd: 1957.9 kJmol−1
3rd: 3666 kJmol−1
Atomic radius 135 pm
Atomic radius (calc.
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cytochrome c oxidase or Complex IV (PDB 2OCC , EC 1.9.3.1 ) is a large transmembrane protein complex found in bacteria and the mitochondrion.
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Function
It is the last protein in the electron transport chain...... Click the link for more information.
3, 4, 6
(amphoteric oxide)
Electronegativity 1.83 (Pauling scale)
Ionization energies
(more) 1st: 762.5 kJmol−1
2nd: 1561.9 kJmol−1
3rd: 2957 kJmol−1
Atomic radius 140 pm
Atomic radius (calc.
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(amphoteric oxide)
Electronegativity 1.83 (Pauling scale)
Ionization energies
(more) 1st: 762.5 kJmol−1
2nd: 1561.9 kJmol−1
3rd: 2957 kJmol−1
Atomic radius 140 pm
Atomic radius (calc.
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Catalase (e.g. human erythrocyte catalase: PDB 1DGF , EC 1.11.1.6 ) is a common enzyme found in living organisms. Its functions include catalyzing the decomposition of hydrogen peroxide to water and oxygen.
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Cytochromes are generally membrane-bound hemoproteins that contain heme groups and carry out electron transport.
They are either found as monomeric proteins (i.e. cytochrome c) or as subunits of bigger enzymatic complexes that catalyze redox reactions.
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They are either found as monomeric proteins (i.e. cytochrome c) or as subunits of bigger enzymatic complexes that catalyze redox reactions.
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A heme or haem is a prosthetic group that consists of an iron atom contained in the center of a large heterocyclic organic ring called a porphyrin. Not all porphyrins contain iron, but a substantial fraction of porphyrin-containing metalloproteins have heme as
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Nitrogenase (EC 1.18.6.1 ) is the enzyme used by some organisms to fix atmospheric nitrogen gas (N2). It is the only known family of enzymes which accomplishes this process.
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A hydrogenase is an enzyme that catalyses the reversible oxidation of molecular hydrogen (H2). Hydrogenases play a vital role in anaerobic metabolism.[1][2]
Hydrogen uptake (H2
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Hydrogen uptake (H2
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2, 3
(mildly basic oxide)
Electronegativity 1.91 (Pauling scale)
Ionization energies
(more) 1st: 737.1 kJmol−1
2nd: 1753.0 kJmol−1
3rd: 3395 kJmol−1
Atomic radius 135 pm
Atomic radius (calc.
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(mildly basic oxide)
Electronegativity 1.91 (Pauling scale)
Ionization energies
(more) 1st: 737.1 kJmol−1
2nd: 1753.0 kJmol−1
3rd: 3395 kJmol−1
Atomic radius 135 pm
Atomic radius (calc.
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Urease (EC 3.5.1.5 ) is an enzyme that catalyzes the hydrolysis of urea into carbon dioxide and ammonia. The reaction occurs as follows:
(NH2)2CO + H2O → CO2 + 2NH3
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(NH2)2CO + H2O → CO2 + 2NH3
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4, 6
(strongly acidic oxide)
Electronegativity 2.55 (scale Pauling)
Ionization energies
(more) 1st: 941.0 kJmol−1
2nd: 2045 kJmol−1
3rd: 2973.
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(strongly acidic oxide)
Electronegativity 2.55 (scale Pauling)
Ionization energies
(more) 1st: 941.0 kJmol−1
2nd: 2045 kJmol−1
3rd: 2973.
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Identifiers
Symbol GPX3
Entrez 2878
HUGO 4555
OMIM 138321
RefSeq NM_002084
UniProt P22352
Other data
EC number 1.11.1.9
Locus Chr.
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Symbol GPX3
Entrez 2878
HUGO 4555
OMIM 138321
RefSeq NM_002084
UniProt P22352
Other data
EC number 1.11.1.9
Locus Chr.
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Zinc (IPA: /ˈzɪŋk/, from German: Zink) is a chemical element in the periodic table that has the symbol Zn and atomic number 30.
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Alcohol dehydrogenases (EC 1.1.1.1 ) are a group of seven dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones.
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