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  2. Catalase - Wikipedia

    en.wikipedia.org/wiki/Catalase

    Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long. [7] It contains four iron-containing heme groups that allow the enzyme to react with hydrogen peroxide. The optimum pH for human catalase is approximately 7, [8] and has a fairly broad maximum: the rate of reaction does not change appreciably between pH 6.8 and 7 ...

  3. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    These conformational changes also bring catalytic residues in the active site close to the chemical bonds in the substrate that will be altered in the reaction. After binding takes place, one or more mechanisms of catalysis lowers the energy of the reaction's transition state, by providing an alternative chemical pathway for the reaction.

  4. Turnover number - Wikipedia

    en.wikipedia.org/wiki/Turnover_number

    In chemistry, the term "turnover number" has two distinct meanings.. In enzymology, the turnover number (k cat) is defined as the limiting number of chemical conversions of substrate molecules per second that a single active site will execute for a given enzyme concentration [E T] for enzymes with two or more active sites. [1]

  5. Catalysis - Wikipedia

    en.wikipedia.org/wiki/Catalysis

    An illustrative example is the effect of catalysts to speed the decomposition of hydrogen peroxide into water and oxygen: . 2 H 2 O 2 → 2 H 2 O + O 2. This reaction proceeds because the reaction products are more stable than the starting compound, but this decomposition is so slow that hydrogen peroxide solutions are commercially available.

  6. Reactive oxygen species - Wikipedia

    en.wikipedia.org/wiki/Reactive_oxygen_species

    Catalase, which is concentrated in peroxisomes located next to mitochondria, reacts with the hydrogen peroxide to catalyze the formation of water and oxygen. Glutathione peroxidase reduces hydrogen peroxide by transferring the energy of the reactive peroxides to a sulfur-containing tripeptide called glutathione. The sulfur contained in these ...

  7. Cofactor (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Cofactor_(biochemistry)

    The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.. A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction).

  8. Catalase-peroxidase - Wikipedia

    en.wikipedia.org/wiki/Catalase-peroxidase

    This enzyme is a strong catalase with H 2 O 2 as donor which releases O 2. References External links. Catalase-peroxidase at the U.S. National Library ...

  9. Peroxidase - Wikipedia

    en.wikipedia.org/wiki/Peroxidase

    Glutathione Peroxidase 1 (Peroxidases or peroxide reductases (EC number 1.11.1.x) are a large group of enzymes which play a role in various biological processes. They are named after the fact that they commonly break up peroxides, and should not be confused with other enzymes that produce peroxide, which are often oxidases.