Catalase: The Constitutional Characteristics Of An Enzyme

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An enzyme is a biological catalyst; they accelerate most reactions within cells (Cooper, 2000). Enzymes have three constitutional characteristics: they assist chemical reactions without becoming exhausted or altered themselves, they do not change the balance between the reactants and products and they are highly specific as to what reactions they are able to catalyse (Cooper, 2000).
The active sites of enzymes are where chemical reactions occur. The active sites are dimples or grooves in the surface of the enzyme, which is composed of amino acids that are brought together in the tertiary structure of the folded protein. Reactants, or substrates, are attracted to the enzyme through hydrogen bonds, ionic bonds and hydrophobic interactions where they then undergo the chemical reaction (Cooper, 2000).
Most enzymes are formed from proteins. Intermolecular forces between the amino acids in the proteins, such as hydrogen bonds, cause the acids to fold into unique forms. The intermolecular forces between different amino acids will differ slightly, causing each amino acid to have a different shape (Brain). This shape affects the shape of the active sites, allowing for their
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Catalase is an enzyme that accelerates the decomposition of hydrogen peroxide into oxygen and water. Catalase is a tetramer, composed of four monomers wrapped into a dumbbell shape (Nguyen). Each monomer has a heme molecule, a part indispensable to the decomposition of hydrogen peroxide. The heme molecule is responsible for binding oxygen. It is disc like in shape and contains an iron atom at their center. In the decomposition of hydrogen peroxide the heme molecule attaches one oxygen atom to its iron atom, the rest of the previously H2O2 molecule is released as H2O (Goodsell, 2004). As a second hydrogen peroxide molecule is bonded to the active site and disassembled, one oxygen atom in combined with the first oxygen atom, releasing O2 gas and H2O (Goodsell,

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